de Vries RP

References (54)

Title : Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl\/acetyl xylan esterases - Dilokpimol_2022_FEBS.Lett__
Author(s) : Dilokpimol A , Verkerk B , Li X , Bellemare A , Lavallee M , Frommhagen M , Normolle Underlin E , Kabel MA , Powlowski J , Tsang A , de Vries RP
Ref : FEBS Letters , : , 2022
Abstract : Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important enzymes for plant biomass degradation and are both present in Carbohydrate Esterase family 1 (CE1) of the Carbohydrate-Active enZymes database. In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced and screened for their activity towards model and complex plant biomass substrates. CE1_1 enzymes possess AXE activity, while CE1_5 enzymes showed FAE activity. Two enzymes from CE1_2 and one from CE1_5 possess dual feruloyl/acetyl xylan esterase (FXE) activity, showing expansion of substrate specificity. The new FXEs from CE1 can efficiently release both feruloyl and acetyl residues from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation. CE1_1 - AXE1B_MYCSE Axe1 MsAxe1 Corse1p7_016869 mycse-axe1b CE1_2 SF6 FAE1B_MYCSE Fxe1 CE1_5 SF5 FAE1C_MYCSE Fae1 MsFae1 Corse1p7_018453 mycse-fae1c CE1_5 SF5 FAE1E_MYCSE Fae2 MsFae2 Corse1p7_001265 mycse-fae1e Non-CE1 SF2 FAE1F_MYCSE Fae3 MsFae3 Corse1p7_018656 mycse-fae1f
ESTHER : Dilokpimol_2022_FEBS.Lett__
PubMedSearch : Dilokpimol_2022_FEBS.Lett__
PubMedID: 35187647
Gene_locus related to this paper: emeni-axe1 , aspng-a0a100iph2 , talem-e9m3d1 , myctt-g2qd29 , chatd-g0sbz2 , chatd-g0s216 , mycse-fae1c , mycse-fae1f , mycse-fae1e , mycse-axe1b , mycse-fae4 , acrth-axe1a , chagb-q2gyn8

Title : Vanillic acid and methoxyhydroquinone production from guaiacyl units and related aromatic compounds using Aspergillus niger cell factories - Lubbers_2021_Microb.Cell.Fact_20_151
Author(s) : Lubbers RJM , Dilokpimol A , Nousiainen PA , Cioc RC , Visser J , Bruijnincx PCA , de Vries RP
Ref : Microb Cell Fact , 20 :151 , 2021
Abstract : BACKGROUND: The aromatic compounds vanillin and vanillic acid are important fragrances used in the food, beverage, cosmetic and pharmaceutical industries. Currently, most aromatic compounds used in products are chemically synthesized, while only a small percentage is extracted from natural sources. The metabolism of vanillin and vanillic acid has been studied for decades in microorganisms and many studies have been conducted that showed that both can be produced from ferulic acid using bacteria. In contrast, the degradation of vanillin and vanillic acid by fungi is poorly studied and no genes involved in this metabolic pathway have been identified. In this study, we aimed to clarify this metabolic pathway in Aspergillus niger and identify the genes involved. RESULTS: Using whole-genome transcriptome data, four genes involved in vanillin and vanillic acid metabolism were identified. These include vanillin dehydrogenase (vdhA), vanillic acid hydroxylase (vhyA), and two genes encoding novel enzymes, which function as methoxyhydroquinone 1,2-dioxygenase (mhdA) and 4-oxo-monomethyl adipate esterase (omeA). Deletion of these genes in A. niger confirmed their role in aromatic metabolism and the enzymatic activities of these enzymes were verified. In addition, we demonstrated that mhdA and vhyA deletion mutants can be used as fungal cell factories for the accumulation of vanillic acid and methoxyhydroquinone from guaiacyl lignin units and related aromatic compounds. CONCLUSIONS: This study provides new insights into the fungal aromatic metabolic pathways involved in the degradation of guaiacyl units and related aromatic compounds. The identification of the involved genes unlocks new potential for engineering aromatic compound-producing fungal cell factories.
ESTHER : Lubbers_2021_Microb.Cell.Fact_20_151
PubMedSearch : Lubbers_2021_Microb.Cell.Fact_20_151
PubMedID: 34344380

Title : From lignocellulose to plastics: Knowledge transfer on the degradation approaches by fungi - Daly_2021_Biotechnol.Adv__107770
Author(s) : Daly P , Cai F , Kubicek CP , Jiang S , Grujic M , Rahimi MJ , Sheteiwy MS , Giles R , Riaz A , de Vries RP , Akcapinar GB , Wei L , Druzhinina IS
Ref : Biotechnol Adv , :107770 , 2021
Abstract : In this review, we argue that there is much to be learned by transferring knowledge from research on lignocellulose degradation to that on plastic. Plastic waste accumulates in the environment to hazardous levels, because it is inherently recalcitrant to biological degradation. Plants evolved lignocellulose to be resistant to degradation, but with time, fungi became capable of utilising it for their nutrition. Examples of how fungal strategies to degrade lignocellulose could be insightful for plastic degradation include how fungi overcome the hydrophobicity of lignin (e.g. production of hydrophobins) and crystallinity of cellulose (e.g. oxidative approaches). In parallel, knowledge of the methods for understanding lignocellulose degradation could be insightful such as advanced microscopy, genomic and post-genomic approaches (e.g. gene expression analysis). The known limitations of biological lignocellulose degradation, such as the necessity for physiochemical pretreatments for biofuel production, can be predictive of potential restrictions of biological plastic degradation. Taking lessons from lignocellulose degradation for plastic degradation is also important for biosafety as engineered plastic-degrading fungi could also have increased plant biomass degrading capabilities. Even though plastics are significantly different from lignocellulose because they lack hydrolysable C-C or C-O bonds and therefore have higher recalcitrance, there are apparent similarities, e.g. both types of compounds are mixtures of hydrophobic polymers with amorphous and crystalline regions, and both require hydrolases and oxidoreductases for their degradation. Thus, many lessons could be learned from fungal lignocellulose degradation.
ESTHER : Daly_2021_Biotechnol.Adv__107770
PubMedSearch : Daly_2021_Biotechnol.Adv__107770
PubMedID: 33989704

Title : Functional Validation of Two Fungal Subfamilies in Carbohydrate Esterase Family 1 by Biochemical Characterization of Esterases From Uncharacterized Branches - Li_2020_Front.Bioeng.Biotechnol_8_694
Author(s) : Li X , Griffin K , Langeveld S , Frommhagen M , Underlin EN , Kabel MA , de Vries RP , Dilokpimol A
Ref : Front Bioeng Biotechnol , 8 :694 , 2020
Abstract : The fungal members of Carbohydrate Esterase family 1 (CE1) from the CAZy database include both acetyl xylan esterases (AXEs) and feruloyl esterases (FAEs). AXEs and FAEs are essential auxiliary enzymes to unlock the full potential of feedstock. They are being used in many biotechnology applications including food and feed, pulp and paper, and biomass valorization. AXEs catalyze the hydrolysis of acetyl group from xylan, while FAEs release ferulic and other hydroxycinnamic acids from xylan and pectin. Previously, we reported a phylogenetic analysis for the fungal members of CE1, establishing five subfamilies (CE1_SF1-SF5). Currently, the characterized AXEs are in the subfamily CE1_SF1, whereas CE1_SF2 contains mainly characterized FAEs. These two subfamilies are more related to each other than to the other subfamilies and are predicted to have evolved from a common ancestor, but target substrates with a different molecular structure. In this study, four ascomycete enzymes from CE1_SF1 and SF2 were heterologously produced in Pichia pastoris and characterized with respect to their biochemical properties and substrate preference toward different model and plant biomass substrates. The selected enzymes from CE1_SF1 only exhibited AXE activity, whereas the one from CE1_SF2 possessed dual FAE/AXE activity. This dual activity enzyme also showed broad substrate specificity toward model substrates for FAE activity and efficiently released both acetic acid and ferulic acid (~50%) from wheat arabinoxylan and wheat bran which was pre-treated with a commercial xylanase. These fungal AXEs and FAEs also showed promising biochemical properties, e.g., high stability over a wide pH range and retaining more than 80% of their residual activity at pH 6.0-9.0. These newly characterized fungal AXEs and FAEs from CE1 have high potential for biotechnological applications. In particular as an additional ingredient for enzyme cocktails to remove the ester-linked decorations which enables access for the backbone degrading enzymes. Among these novel enzymes, the dual FAE/AXE activity enzyme also supports the evolutionary relationship of CE1_SF1 and SF2.
ESTHER : Li_2020_Front.Bioeng.Biotechnol_8_694
PubMedSearch : Li_2020_Front.Bioeng.Biotechnol_8_694
PubMedID: 32671051

Title : Feruloyl Esterases for Biorefineries: Subfamily Classified Specificity for Natural Substrates - Underlin_2020_Front.Bioeng.Biotechnol_8_332
Author(s) : Underlin EN , Frommhagen M , Dilokpimol A , van Erven G , de Vries RP , Kabel MA
Ref : Front Bioeng Biotechnol , 8 :332 , 2020
Abstract : Feruloyl esterases (FAEs) have an important role in the enzymatic conversion of lignocellulosic biomass by decoupling plant cell wall polysaccharides and lignin. Moreover, FAEs release anti-oxidative hydroxycinnamic acids (HCAs) from biomass. As a plethora of FAE candidates were found in fungal genomes, FAE classification related to substrate specificity is an indispensability for selection of most suitable candidates. Hence, linking distinct substrate specificities to a FAE classification, such as the recently classified FAE subfamilies (SF), is a promising approach to improve the application of these enzymes for a variety of industrial applications. In total, 14 FAEs that are classified members of SF1, 5, 6, 7, 9, and 13 were tested in this research. All FAEs were investigated for their activity toward a variety of substrates: synthetic model substrates, plant cell wall-derived substrates, including lignin, and natural substrates. Released HCAs were determined using reverse phase-ultra high performance liquid chromatography coupled to UV detection and mass spectrometry. Based on this study, FAEs of SF5 and SF7 showed the highest release of FA, pCA, and diFAs over the range of substrates, while FAEs of SF6 were comparable but less pronounced for diFAs release. These results suggest that SF5 and SF7 FAEs are promising enzymes for biorefinery applications, like the production of biofuels, where a complete degradation of the plant cell wall is desired. In contrast, SF6 FAEs might be of interest for industrial applications that require a high release of only FA and pCA, which are needed as precursors for the production of biochemicals. In contrast, FAEs of SF1, 9 and 13 showed an overall low release of HCAs from plant cell wall-derived and natural substrates. The obtained results substantiate the previous SF classification as a useful tool to predict the substrate specificity of FAEs, which eases the selection of FAE candidates for industrial applications.
ESTHER : Underlin_2020_Front.Bioeng.Biotechnol_8_332
PubMedSearch : Underlin_2020_Front.Bioeng.Biotechnol_8_332
PubMedID: 32391342
Gene_locus related to this paper: stehr-ShFae1 , 9euro-a0a1l9t4i5 , aspng-AnFaeJ , 9euro-a0a1l9t9j3 , 9euro-a0a1l9txk3 , myctt-faeb , aspnc-faec , aspni-FAEA , 9euro-a0a1l9tdb5 , myctt-g2qmb4 , 9euro-g4xkn5

Title : Genomic and Genetic Insights Into a Cosmopolitan Fungus, Paecilomyces variotii (Eurotiales) - Urquhart_2018_Front.Microbiol_9_3058
Author(s) : Urquhart AS , Mondo SJ , Makela MR , Hane JK , Wiebenga A , He G , Mihaltcheva S , Pangilinan J , Lipzen A , Barry K , de Vries RP , Grigoriev IV , Idnurm A
Ref : Front Microbiol , 9 :3058 , 2018
Abstract : Species in the genus Paecilomyces, a member of the fungal order Eurotiales, are ubiquitous in nature and impact a variety of human endeavors. Here, the biology of one common species, Paecilomyces variotii, was explored using genomics and functional genetics. Sequencing the genome of two isolates revealed key genome and gene features in this species. A striking feature of the genome was the two-part nature, featuring large stretches of DNA with normal GC content separated by AT-rich regions, a hallmark of many plant-pathogenic fungal genomes. These AT-rich regions appeared to have been mutated by repeat-induced point (RIP) mutations. We developed methods for genetic transformation of P. variotii, including forward and reverse genetics as well as crossing techniques. Using transformation and crossing, RIP activity was identified, demonstrating for the first time that RIP is an active process within the order Eurotiales. A consequence of RIP is likely reflected by a reduction in numbers of genes within gene families, such as in cell wall degradation, and reflected by growth limitations on P. variotii on diverse carbon sources. Furthermore, using these transformation tools we characterized a conserved protein containing a domain of unknown function (DUF1212) and discovered it is involved in pigmentation.
ESTHER : Urquhart_2018_Front.Microbiol_9_3058
PubMedSearch : Urquhart_2018_Front.Microbiol_9_3058
PubMedID: 30619145
Gene_locus related to this paper: byssp-a0a443i770 , byssp-a0a443i5x3 , byssp-vdta1

Title : The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has shifted to a protein diet - Grum-Grzhimaylo_2018_Mol.Ecol_27_4808
Author(s) : Grum-Grzhimaylo AA , Falkoski DL , van den Heuvel J , Valero-Jimenez CA , Min B , Choi IG , Lipzen A , Daum CG , Aanen DK , Tsang A , Henrissat B , Bilanenko EN , de Vries RP , van Kan JAL , Grigoriev IV , Debets AJM
Ref : Mol Ecol , 27 :4808 , 2018
Abstract : Sodiomyces alkalinus is one of the very few alkalophilic fungi, adapted to grow optimally at high pH. It is widely distributed at the plant-deprived edges of extremely alkaline lakes and locally abundant. We sequenced the genome of S. alkalinus and reconstructed evolution of catabolic enzymes, using a phylogenomic comparison. We found that the genome of S. alkalinus is larger, but its predicted proteome is smaller and heavily depleted of both plant-degrading enzymes and proteinases, when compared to its closest plant-pathogenic relatives. Interestingly, despite overall losses, S. alkalinus has retained many proteinases families and acquired bacterial cell wall-degrading enzymes, some of them via horizontal gene transfer from bacteria. This fungus has very potent proteolytic activity at high pH values, but slowly induced low activity of cellulases and hemicellulases. Our experimental and in silico data suggest that plant biomass, a common food source for most fungi, is not a preferred substrate for S. alkalinus in its natural environment. We conclude that the fungus has abandoned the ancestral plant-based diet and has become specialized in a more protein-rich food, abundantly available in soda lakes in the form of prokaryotes and small crustaceans.
ESTHER : Grum-Grzhimaylo_2018_Mol.Ecol_27_4808
PubMedSearch : Grum-Grzhimaylo_2018_Mol.Ecol_27_4808
PubMedID: 30368956
Gene_locus related to this paper: 9pezi-a0a3n2q0e7 , 9pezi-a0a3n2pu70 , 9pezi-a0a3n2puy7

Title : Fungal glucuronoyl esterases: Genome mining based enzyme discovery and biochemical characterization - Dilokpimol_2018_N.Biotechnol_40_282
Author(s) : Dilokpimol A , Makela MR , Cerullo G , Zhou M , Varriale S , Gidijala L , Bras JLA , Jutten P , Piechot A , Verhaert R , Faraco V , Hilden KS , de Vries RP
Ref : N Biotechnol , 40 :282 , 2018
Abstract : 4-O-Methyl-d-glucuronic acid (MeGlcA) is a side-residue of glucuronoarabinoxylan and can form ester linkages to lignin, contributing significantly to the strength and rigidity of the plant cell wall. Glucuronoyl esterases (4-O-methyl-glucuronoyl methylesterases, GEs) can cleave this ester bond, and therefore may play a significant role as auxiliary enzymes in biomass saccharification for the production of biofuels and biochemicals. GEs belong to a relatively new family of carbohydrate esterases (CE15) in the CAZy database (, and so far around ten fungal GEs have been characterized. To explore additional GE enzymes, we used a genome mining strategy. BLAST analysis with characterized GEs against approximately 250 publicly accessible fungal genomes identified more than 150 putative fungal GEs, which were classified into eight phylogenetic sub-groups. To validate the genome mining strategy, 21 selected GEs from both ascomycete and basidiomycete fungi were heterologously produced in Pichia pastoris. Of these enzymes, 18 were active against benzyl d-glucuronate demonstrating the suitability of our genome mining strategy for enzyme discovery.
ESTHER : Dilokpimol_2018_N.Biotechnol_40_282
PubMedSearch : Dilokpimol_2018_N.Biotechnol_40_282
PubMedID: 29051046

Title : Characterization of a feruloyl esterase from Aspergillus terreus facilitates the division of fungal enzymes from Carbohydrate Esterase family 1 of the carbohydrate-active enzymes (CAZy) database - Makela_2018_Microb.Biotechnol_11_869
Author(s) : Makela MR , Dilokpimol A , Koskela SM , Kuuskeri J , de Vries RP , Hilden K
Ref : Microb Biotechnol , 11 :869 , 2018
Abstract : Feruloyl esterases (FAEs) are accessory enzymes for plant biomass degradation, which catalyse hydrolysis of carboxylic ester linkages between hydroxycinnamic acids and plant cell-wall carbohydrates. They are a diverse group of enzymes evolved from, e.g. acetyl xylan esterases (AXEs), lipases and tannases, thus complicating their classification and prediction of function by sequence similarity. Recently, an increasing number of fungal FAEs have been biochemically characterized, owing to their potential in various biotechnological applications and multitude of candidate FAEs in fungal genomes. However, only part of the fungal FAEs are included in Carbohydrate Esterase family 1 (CE1) of the carbohydrate-active enzymes (CAZy) database. In this work, we performed a phylogenetic analysis that divided the fungal members of CE1 into five subfamilies of which three contained characterized enzymes with conserved activities. Conservation within one of the subfamilies was confirmed by characterization of an additional CE1 enzyme from Aspergillus terreus. Recombinant A. terreus FaeD (AtFaeD) showed broad specificity towards synthetic methyl and ethyl esters, and released ferulic acid from plant biomass substrates, demonstrating its true FAE activity and interesting features as potential biocatalyst. The subfamily division of the fungal CE1 members enables more efficient selection of candidate enzymes for biotechnological processes.
ESTHER : Makela_2018_Microb.Biotechnol_11_869
PubMedSearch : Makela_2018_Microb.Biotechnol_11_869
PubMedID: 29697197
Gene_locus related to this paper: asptn-q0ci40

Title : Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies - Dilokpimol_2018_N.Biotechnol_41_9
Author(s) : Dilokpimol A , Makela MR , Varriale S , Zhou M , Cerullo G , Gidijala L , Hinkka H , Bras JLA , Jutten P , Piechot A , Verhaert R , Hilden KS , Faraco V , de Vries RP
Ref : N Biotechnol , 41 :9 , 2018
Abstract : Feruloyl esterases (FAEs) are a diverse group of enzymes that specifically catalyze the hydrolysis of ester bonds between a hydroxycinnamic (e.g. ferulic) acid and plant poly- or oligosaccharides. FAEs as auxiliary enzymes significantly assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass saccharification for biofuel and biochemical production. A limited number of FAEs have been functionally characterized compared to over 1000 putative fungal FAEs that were recently predicted by similarity-based genome mining, which divided phylogenetically into different subfamilies (SFs). In this study, 27 putative and six characterized FAEs from both ascomycete and basidiomycete fungi were selected and heterologously expressed in Pichia pastoris and the recombinant proteins biochemically characterized to validate the previous genome mining and phylogenetical grouping and to expand the information on activity of fungal FAEs. As a result, 20 enzymes were shown to possess FAE activity, being active towards pNP-ferulate and/or methyl hydroxycinnamate substrates, and covering 11 subfamilies. Most of the new FAEs showed activities comparable to those of previously characterized fungal FAEs.
ESTHER : Dilokpimol_2018_N.Biotechnol_41_9
PubMedSearch : Dilokpimol_2018_N.Biotechnol_41_9
PubMedID: 29174720
Gene_locus related to this paper: aspng-a0a100iph2

Title : Expanding the feruloyl esterase gene family of Aspergillus niger by characterization of a feruloyl esterase, FaeC - Dilokpimol_2017_N.Biotechnol_37_200
Author(s) : Dilokpimol A , Makela MR , Mansouri S , Belova O , Waterstraat M , Bunzel M , de Vries RP , Hilden KS
Ref : N Biotechnol , 37 :200 , 2017
Abstract : A feruloyl esterase (FAE) from Aspergillus niger N402, FaeC was heterologously produced in Pichia pastoris X-33 in a yield of 10mg/L. FaeC was most active at pH 7.0 and 50 degrees C, and showed broad substrate specificity and catalyzed the hydrolysis of methyl 3,4-dimethoxycinnamate, ethyl ferulate, methyl ferulate, methyl p-coumarate, ethyl coumarate, methyl sinapate, and methyl caffeate. The enzyme released both ferulic acid and p-coumaric acid from wheat arabinoxylan and sugar beet pectin (up to 3mg/g polysaccharide), and acted synergistically with a commercial xylanase increasing the release of ferulic acid up to six-fold. The expression of faeC increased over time in the presence of feruloylated polysaccharides. Cinnamic, syringic, caffeic, vanillic and ferulic acid induced the expression of faeC. Overall expression of faeC was very low in all tested conditions, compared to two other A. niger FAE encoding genes, faeA and faeB. Our data showed that the fae genes responded differently towards the feruloylated polysaccharides and tested monomeric phenolic compounds suggesting that the corresponding FAE isoenzymes may target different substrates in a complementary manner. This may increase the efficiency of the degradation of diverse plant biomass.
ESTHER : Dilokpimol_2017_N.Biotechnol_37_200
PubMedSearch : Dilokpimol_2017_N.Biotechnol_37_200
PubMedID: 28285179
Gene_locus related to this paper: aspnc-faec

Title : Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds - Huttner_2017_Appl.Microbiol.Biotechnol_101_5301
Author(s) : Huttner S , Klaubauf S , de Vries RP , Olsson L
Ref : Applied Microbiology & Biotechnology , 101 :5301 , 2017
Abstract : The glucuronoyl esterases (GEs) that have been identified so far belong to family 15 of the carbohydrate esterases in the CAZy classification system and are presumed to target ester bonds between lignin alcohols and (4-O-methyl-)D-glucuronic acid residues of xylan. Few GEs have been cloned, expressed and characterised to date. Characterisation has been done on a variety of synthetic substrates; however, the number of commercially available substrates is very limited. We identified novel putative GEs from a wide taxonomic range of fungi and expressed the enzymes originating from Acremonium alcalophilum and Wolfiporia cocos as well as the previously described PcGE1 from Phanerochaete chrysosporium. All three fungal GEs were active on the commercially available compounds benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree on methyl glucuronic acid (MeGlcA). The enzymes showed pH stability over a wide pH range and tolerated 6-h incubations of up to 50 degreesC. Kinetic parameters were determined for BnGlcA. This study shows the suitability of the commercially available model compounds BnGlcA, MeGlcA and allylGlcA in GE activity screening and characterisation experiments. We enriched the spectrum of characterised GEs with two new members of a relatively young enzyme family. Due to its biotechnological significance, this family deserves to be more extensively studied. The presented enzymes are promising candidates as auxiliary enzymes to improve saccharification of plant biomass.
ESTHER : Huttner_2017_Appl.Microbiol.Biotechnol_101_5301
PubMedSearch : Huttner_2017_Appl.Microbiol.Biotechnol_101_5301
PubMedID: 28429057
Gene_locus related to this paper: wolco-gce1 , acram-a0a1d8ejg8 , phacr-gce1 , phacr-gce2

Title : Comparative genomics reveals high biological diversity and specific adaptations in the industrially and medically important fungal genus Aspergillus - de Vries_2017_Genome.Biol_18_28
Author(s) : de Vries RP , Riley R , Wiebenga A , Aguilar-Osorio G , Amillis S , Uchima CA , Anderluh G , Asadollahi M , Askin M , Barry K , Battaglia E , Bayram O , Benocci T , Braus-Stromeyer SA , Caldana C , Canovas D , Cerqueira GC , Chen F , Chen W , Choi C , Clum A , Dos Santos RA , Damasio AR , Diallinas G , Emri T , Fekete E , Flipphi M , Freyberg S , Gallo A , Gournas C , Habgood R , Hainaut M , Harispe ML , Henrissat B , Hilden KS , Hope R , Hossain A , Karabika E , Karaffa L , Karanyi Z , Krasevec N , Kuo A , Kusch H , LaButti K , Lagendijk EL , Lapidus A , Levasseur A , Lindquist E , Lipzen A , Logrieco AF , Maccabe A , Makela MR , Malavazi I , Melin P , Meyer V , Mielnichuk N , Miskei M , Molnar AP , Mule G , Ngan CY , Orejas M , Orosz E , Ouedraogo JP , Overkamp KM , Park HS , Perrone G , Piumi F , Punt PJ , Ram AF , Ramon A , Rauscher S , Record E , Riano-Pachon DM , Robert V , Rohrig J , Ruller R , Salamov A , Salih NS , Samson RA , Sandor E , Sanguinetti M , Schutze T , Sepcic K , Shelest E , Sherlock G , Sophianopoulou V , Squina FM , Sun H , Susca A , Todd RB , Tsang A , Unkles SE , van de Wiele N , van Rossen-Uffink D , Oliveira JV , Vesth TC , Visser J , Yu JH , Zhou M , Andersen MR , Archer DB , Baker SE , Benoit I , Brakhage AA , Braus GH , Fischer R , Frisvad JC , Goldman GH , Houbraken J , Oakley B , Pocsi I , Scazzocchio C , Seiboth B , vanKuyk PA , Wortman J , Dyer PS , Grigoriev IV
Ref : Genome Biol , 18 :28 , 2017
Abstract : BACKGROUND: The fungal genus Aspergillus is of critical importance to humankind. Species include those with industrial applications, important pathogens of humans, animals and crops, a source of potent carcinogenic contaminants of food, and an important genetic model. The genome sequences of eight aspergilli have already been explored to investigate aspects of fungal biology, raising questions about evolution and specialization within this genus. RESULTS: We have generated genome sequences for ten novel, highly diverse Aspergillus species and compared these in detail to sister and more distant genera. Comparative studies of key aspects of fungal biology, including primary and secondary metabolism, stress response, biomass degradation, and signal transduction, revealed both conservation and diversity among the species. Observed genomic differences were validated with experimental studies. This revealed several highlights, such as the potential for sex in asexual species, organic acid production genes being a key feature of black aspergilli, alternative approaches for degrading plant biomass, and indications for the genetic basis of stress response. A genome-wide phylogenetic analysis demonstrated in detail the relationship of the newly genome sequenced species with other aspergilli. CONCLUSIONS: Many aspects of biological differences between fungal species cannot be explained by current knowledge obtained from genome sequences. The comparative genomics and experimental study, presented here, allows for the first time a genus-wide view of the biological diversity of the aspergilli and in many, but not all, cases linked genome differences to phenotype. Insights gained could be exploited for biotechnological and medical applications of fungi.
ESTHER : de Vries_2017_Genome.Biol_18_28
PubMedSearch : de Vries_2017_Genome.Biol_18_28
PubMedID: 28196534
Gene_locus related to this paper: asptu-a0a1l9nhd0 , aspve-a0a1l9pxx8 , aspve-a0a1l9q4m3 , aspwe-a0a1l9s133 , 9euro-a0a1l9t3v9 , aspwe-a0a1l9rcx6 , aspna-g3y5a6 , aspgl-a0a1l9v4d3 , 9euro-a0a1l9sa36 , aspsb-a0a319eji6 , aspve-a0a1l9px96 , 9euro-a0a1l9tay1 , aspgl-a0a1l9vbc0 , aspc5-a0a1r3rh65 , 9euro-a0a2v5i956 , aspwe-a0a1l9rpp6 , aspna-g3xpw9 , aspve-a0a1l9plv1 , 9euro-a0a1l9tk47 , aspve-a0a1l9pde9 , aspve-a0a1l9pz72 , aspwe-a0a1l9rde6 , 9euro-a0a1l9tdb5 , aspkw-g7xq95 , aspbc-a0a1l9u6h4 , aspbc-a0a1l9u2l4 , asptc-a0a1l9mx83 , aspgl-a0a1l9ve90 , aspve-a0a1l9pvz9 , 9euro-a0a1l9tdh3 , aspc5-a0a1r3rmn9 , aspwe-a0a1l9rlq2 , asptc-a0a1l9nby7 , aspng-a0a100i8t9 , aspc5-a0a1r3rem6 , aspbc-a0a1l9uy89 , aspa1-anee , aspa1-aneh , aspa1-acrc , aspbc-alba , aspa1-acui

Title : Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications - Dilokpimol_2016_Biotechnol.Biofuels_9_231
Author(s) : Dilokpimol A , Makela MR , Aguilar-Pontes MV , Benoit-Gelber I , Hilden KS , de Vries RP
Ref : Biotechnol Biofuels , 9 :231 , 2016
Abstract : Feruloyl esterases (FAEs) represent a diverse group of carboxyl esterases that specifically catalyze the hydrolysis of ester bonds between ferulic (hydroxycinnamic) acid and plant cell wall polysaccharides. Therefore, FAEs act as accessory enzymes to assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass conversion. Their ability to release ferulic acid and other hydroxycinnamic acids from plant biomass makes FAEs potential biocatalysts in a wide variety of applications such as in biofuel, food and feed, pulp and paper, cosmetics, and pharmaceutical industries. This review provides an updated overview of the knowledge on fungal FAEs, in particular describing their role in plant biomass degradation, diversity of their biochemical properties and substrate specificities, their regulation and conditions needed for their induction. Furthermore, the discovery of new FAEs using genome mining and phylogenetic analysis of current publicly accessible fungal genomes will also be presented. This has led to a new subfamily classification of fungal FAEs that takes into account both phylogeny and substrate specificity.
ESTHER : Dilokpimol_2016_Biotechnol.Biofuels_9_231
PubMedSearch : Dilokpimol_2016_Biotechnol.Biofuels_9_231
PubMedID: 27795736
Gene_locus related to this paper: stehr-ShFae1 , 9euro-a0a1l9t4i5 , aspng-AnFaeJ , 9euro-a0a1l9t9j3 , 9euro-a0a1l9txk3 , myctt-faeb , aspni-FAEA , 9euro-a0a1l9tdb5 , myctt-g2qmb4 , 9euro-g4xkn5

Title : Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P. chrysosporium, to elucidate the genetic basis of the distinct wood types they colonize - Suzuki_2012_BMC.Genomics_13_444
Author(s) : Suzuki H , MacDonald J , Syed K , Salamov A , Hori C , Aerts A , Henrissat B , Wiebenga A , vanKuyk PA , Barry K , Lindquist E , LaButti K , Lapidus A , Lucas S , Coutinho P , Gong Y , Samejima M , Mahadevan R , Abou-Zaid M , de Vries RP , Igarashi K , Yadav JS , Grigoriev IV , Master ER
Ref : BMC Genomics , 13 :444 , 2012
Abstract : BACKGROUND: Softwood is the predominant form of land plant biomass in the Northern hemisphere, and is among the most recalcitrant biomass resources to bioprocess technologies. The white rot fungus, Phanerochaete carnosa, has been isolated almost exclusively from softwoods, while most other known white-rot species, including Phanerochaete chrysosporium, were mainly isolated from hardwoods. Accordingly, it is anticipated that P. carnosa encodes a distinct set of enzymes and proteins that promote softwood decomposition. To elucidate the genetic basis of softwood bioconversion by a white-rot fungus, the present study reports the P. carnosa genome sequence and its comparative analysis with the previously reported P. chrysosporium genome.
RESULTS: P. carnosa encodes a complete set of lignocellulose-active enzymes. Comparative genomic analysis revealed that P. carnosa is enriched with genes encoding manganese peroxidase, and that the most divergent glycoside hydrolase families were predicted to encode hemicellulases and glycoprotein degrading enzymes. Most remarkably, P. carnosa possesses one of the largest P450 contingents (266 P450s) among the sequenced and annotated wood-rotting basidiomycetes, nearly double that of P. chrysosporium. Along with metabolic pathway modeling, comparative growth studies on model compounds and chemical analyses of decomposed wood components showed greater tolerance of P. carnosa to various substrates including coniferous heartwood.
CONCLUSIONS: The P. carnosa genome is enriched with genes that encode P450 monooxygenases that can participate in extractives degradation, and manganese peroxidases involved in lignin degradation. The significant expansion of P450s in P. carnosa, along with differences in carbohydrate- and lignin-degrading enzymes, could be correlated to the utilization of heartwood and sapwood preparations from both coniferous and hardwood species.
ESTHER : Suzuki_2012_BMC.Genomics_13_444
PubMedSearch : Suzuki_2012_BMC.Genomics_13_444
PubMedID: 22937793
Gene_locus related to this paper: phacs-k5whx2 , phacs-k5v2s8 , phacs-k5v5r2 , phacs-k5vyk5 , phacs-k5vzf8 , phacs-k5wbu9 , phacs-k5wc10 , phacs-k5wpw0 , phacs-k5wzn6 , phacs-k5x1t8 , phacs-k5x5g6 , phacs-k5x5p4

Title : Genome sequence of the button mushroom Agaricus bisporus reveals mechanisms governing adaptation to a humic-rich ecological niche - Morin_2012_Proc.Natl.Acad.Sci.U.S.A_109_17501
Author(s) : Morin E , Kohler A , Baker AR , Foulongne-Oriol M , Lombard V , Nagy LG , Ohm RA , Patyshakuliyeva A , Brun A , Aerts AL , Bailey AM , Billette C , Coutinho PM , Deakin G , Doddapaneni H , Floudas D , Grimwood J , Hilden K , Kues U , LaButti KM , Lapidus A , Lindquist EA , Lucas SM , Murat C , Riley RW , Salamov AA , Schmutz J , Subramanian V , Wosten HA , Xu J , Eastwood DC , Foster GD , Sonnenberg AS , Cullen D , de Vries RP , Lundell T , Hibbett DS , Henrissat B , Burton KS , Kerrigan RW , Challen MP , Grigoriev IV , Martin F
Ref : Proc Natl Acad Sci U S A , 109 :17501 , 2012
Abstract : Agaricus bisporus is the model fungus for the adaptation, persistence, and growth in the humic-rich leaf-litter environment. Aside from its ecological role, A. bisporus has been an important component of the human diet for over 200 y and worldwide cultivation of the "button mushroom" forms a multibillion dollar industry. We present two A. bisporus genomes, their gene repertoires and transcript profiles on compost and during mushroom formation. The genomes encode a full repertoire of polysaccharide-degrading enzymes similar to that of wood-decayers. Comparative transcriptomics of mycelium grown on defined medium, casing-soil, and compost revealed genes encoding enzymes involved in xylan, cellulose, pectin, and protein degradation are more highly expressed in compost. The striking expansion of heme-thiolate peroxidases and beta-etherases is distinctive from Agaricomycotina wood-decayers and suggests a broad attack on decaying lignin and related metabolites found in humic acid-rich environment. Similarly, up-regulation of these genes together with a lignolytic manganese peroxidase, multiple copper radical oxidases, and cytochrome P450s is consistent with challenges posed by complex humic-rich substrates. The gene repertoire and expression of hydrolytic enzymes in A. bisporus is substantially different from the taxonomically related ectomycorrhizal symbiont Laccaria bicolor. A common promoter motif was also identified in genes very highly expressed in humic-rich substrates. These observations reveal genetic and enzymatic mechanisms governing adaptation to the humic-rich ecological niche formed during plant degradation, further defining the critical role such fungi contribute to soil structure and carbon sequestration in terrestrial ecosystems. Genome sequence will expedite mushroom breeding for improved agronomic characteristics.
ESTHER : Morin_2012_Proc.Natl.Acad.Sci.U.S.A_109_17501
PubMedSearch : Morin_2012_Proc.Natl.Acad.Sci.U.S.A_109_17501
PubMedID: 23045686
Gene_locus related to this paper: agabu-k5x1b4 , agabu-k5x521 , agabu-k5w389 , agabu-k5wbk9 , agabu-k5wrh0 , agabu-k5ws85 , agabu-k5wsf9 , agabu-k5wxv1 , agabu-k5x0d9 , agabu-k5x588 , agabu-k5x5x2 , agabu-k5xd51 , agabu-k5xh54 , agabu-k5xsm1 , agabu-k5xsp8 , agabu-k5xtc1 , agabu-k5y2v2 , agabb-k9i3g9 , agabb-k9hnv7 , agabb-k9hr46 , agabu-k5wys0

Title : The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes - Floudas_2012_Science_336_1715
Author(s) : Floudas D , Binder M , Riley R , Barry K , Blanchette RA , Henrissat B , Martinez AT , Otillar R , Spatafora JW , Yadav JS , Aerts A , Benoit I , Boyd A , Carlson A , Copeland A , Coutinho PM , de Vries RP , Ferreira P , Findley K , Foster B , Gaskell J , Glotzer D , Gorecki P , Heitman J , Hesse C , Hori C , Igarashi K , Jurgens JA , Kallen N , Kersten P , Kohler A , Kues U , Kumar TK , Kuo A , LaButti K , Larrondo LF , Lindquist E , Ling A , Lombard V , Lucas S , Lundell T , Martin R , McLaughlin DJ , Morgenstern I , Morin E , Murat C , Nagy LG , Nolan M , Ohm RA , Patyshakuliyeva A , Rokas A , Ruiz-Duenas FJ , Sabat G , Salamov A , Samejima M , Schmutz J , Slot JC , St John F , Stenlid J , Sun H , Sun S , Syed K , Tsang A , Wiebenga A , Young D , Pisabarro A , Eastwood DC , Martin F , Cullen D , Grigoriev IV , Hibbett DS
Ref : Science , 336 :1715 , 2012
Abstract : Wood is a major pool of organic carbon that is highly resistant to decay, owing largely to the presence of lignin. The only organisms capable of substantial lignin decay are white rot fungi in the Agaricomycetes, which also contains non-lignin-degrading brown rot and ectomycorrhizal species. Comparative analyses of 31 fungal genomes (12 generated for this study) suggest that lignin-degrading peroxidases expanded in the lineage leading to the ancestor of the Agaricomycetes, which is reconstructed as a white rot species, and then contracted in parallel lineages leading to brown rot and mycorrhizal species. Molecular clock analyses suggest that the origin of lignin degradation might have coincided with the sharp decrease in the rate of organic carbon burial around the end of the Carboniferous period.
ESTHER : Floudas_2012_Science_336_1715
PubMedSearch : Floudas_2012_Science_336_1715
PubMedID: 22745431
Gene_locus related to this paper: aurde-j0d098 , aurde-j0dc31 , glota-s7rlc1 , fompi-s8f7s4 , dacsp-m5fpg2 , dicsq-r7sm16 , dacsp-m5g7q5 , dacsp-m5fr12 , glota-s7q5w3 , fompi-s8f826.1 , fompi-s8f826.2 , dicsq-r7sy09 , glota-s7rt87 , dicsq-r7t032 , glota-s7rym7 , fompi-s8fiv2 , dacsp-m5gda3.2 , dicsq-r7swi6 , dacsp-m5frf2 , fompi-s8ebb6 , dicsq-r7sln3 , dicsq-r7sya6 , dacsp-m5g7g1 , dicsq-r7syx7 , dicsq-r7sx57 , dacsp-m5fps7 , glota-s7pwi7 , dicsq-r7swj6 , fompi-s8ejq6 , dicsq-r7spc3 , glota-s7q258 , dacsp-m5ft65 , glota-s7q3m7 , fompi-s8dkc7 , glota-s7q1z1 , fompi-s8eqi2 , glota-s7q1z8 , fompi-s8du50 , dacsp-m5gg33 , dacsp-m5g3a7 , fompi-s8ecd7 , fompi-s8dps1 , dacsp-m5fwr0 , dicsq-r7sub7 , glota-s7q8k9 , fompi-s8ffc3 , dacsp-m5g2f9 , fompi-s8ecc2 , dacsp-m5g868 , fompi-s8f890 , dicsq-r7t1a8 , fompi-s8ebx4 , fompi-s8eb97 , glota-s7q222 , glota-s7puf0 , fompi-s8f6v9 , dacsp-m5g0z2 , dacsp-m5gdh9 , fompi-s8fb37 , dacsp-m5fy91 , glota-s7q5v6 , fompi-s8fl44 , dicsq-r7stv9 , dicsq-r7szk3 , fompi-s8epq9 , glota-s7rh56 , dacsp-m5gbt1 , punst-r7s3x9 , punst-r7s0t5 , glota-s7q312 , glota-s7rhh6 , dicsq-r7t117 , dicsq-r7slz3

Title : The genomes of the fungal plant pathogens Cladosporium fulvum and Dothistroma septosporum reveal adaptation to different hosts and lifestyles but also signatures of common ancestry - de Wit_2012_PLoS.Genet_8_E1003088
Author(s) : de Wit PJ , van der Burgt A , Okmen B , Stergiopoulos I , Abd-Elsalam KA , Aerts AL , Bahkali AH , Beenen HG , Chettri P , Cox MP , Datema E , de Vries RP , Dhillon B , Ganley AR , Griffiths SA , Guo Y , Hamelin RC , Henrissat B , Kabir MS , Jashni MK , Kema G , Klaubauf S , Lapidus A , Levasseur A , Lindquist E , Mehrabi R , Ohm RA , Owen TJ , Salamov A , Schwelm A , Schijlen E , Sun H , van den Burg HA , van Ham RC , Zhang S , Goodwin SB , Grigoriev IV , Collemare J , Bradshaw RE
Ref : PLoS Genet , 8 :e1003088 , 2012
Abstract : We sequenced and compared the genomes of the Dothideomycete fungal plant pathogens Cladosporium fulvum (Cfu) (syn. Passalora fulva) and Dothistroma septosporum (Dse) that are closely related phylogenetically, but have different lifestyles and hosts. Although both fungi grow extracellularly in close contact with host mesophyll cells, Cfu is a biotroph infecting tomato, while Dse is a hemibiotroph infecting pine. The genomes of these fungi have a similar set of genes (70% of gene content in both genomes are homologs), but differ significantly in size (Cfu >61.1-Mb; Dse 31.2-Mb), which is mainly due to the difference in repeat content (47.2% in Cfu versus 3.2% in Dse). Recent adaptation to different lifestyles and hosts is suggested by diverged sets of genes. Cfu contains an alpha-tomatinase gene that we predict might be required for detoxification of tomatine, while this gene is absent in Dse. Many genes encoding secreted proteins are unique to each species and the repeat-rich areas in Cfu are enriched for these species-specific genes. In contrast, conserved genes suggest common host ancestry. Homologs of Cfu effector genes, including Ecp2 and Avr4, are present in Dse and induce a Cf-Ecp2- and Cf-4-mediated hypersensitive response, respectively. Strikingly, genes involved in production of the toxin dothistromin, a likely virulence factor for Dse, are conserved in Cfu, but their expression differs markedly with essentially no expression by Cfu in planta. Likewise, Cfu has a carbohydrate-degrading enzyme catalog that is more similar to that of necrotrophs or hemibiotrophs and a larger pectinolytic gene arsenal than Dse, but many of these genes are not expressed in planta or are pseudogenized. Overall, comparison of their genomes suggests that these closely related plant pathogens had a common ancestral host but since adapted to different hosts and lifestyles by a combination of differentiated gene content, pseudogenization, and gene regulation.
ESTHER : de Wit_2012_PLoS.Genet_8_E1003088
PubMedSearch : de Wit_2012_PLoS.Genet_8_E1003088
PubMedID: 23209441
Gene_locus related to this paper: mycpj-q30dw8 , mycp1-n1pnd6 , mycp1-n1per0 , mycp1-n1pg49 , mycp1-n1pwj1 , mycp1-n1pcl8 , mycp1-m2y2b1 , mycp1-n1pwu7 , mycp1-n1ppa8 , mycp1-m2yk59 , mycp1-n1pps5 , mycp1-n1pw13 , mycp1-n1pe19 , mycp1-m2xhl1 , mycp1-n1pnh6 , mycp1-n1psn5 , mycp1-n1puh9 , mycp1-n1phf7 , mycp1-m2y2h4 , mycp1-n1q523 , dotsn-n1q1b1 , dotsn-n1q415 , dotsn-est1

Title : Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis - Fernandez-Fueyo_2012_Proc.Natl.Acad.Sci.U.S.A_109_5458
Author(s) : Fernandez-Fueyo E , Ruiz-Duenas FJ , Ferreira P , Floudas D , Hibbett DS , Canessa P , Larrondo LF , James TY , Seelenfreund D , Lobos S , Polanco R , Tello M , Honda Y , Watanabe T , Ryu JS , Kubicek CP , Schmoll M , Gaskell J , Hammel KE , St John FJ , Vanden Wymelenberg A , Sabat G , Splinter BonDurant S , Syed K , Yadav JS , Doddapaneni H , Subramanian V , Lavin JL , Oguiza JA , Perez G , Pisabarro AG , Ramirez L , Santoyo F , Master E , Coutinho PM , Henrissat B , Lombard V , Magnuson JK , Kues U , Hori C , Igarashi K , Samejima M , Held BW , Barry KW , LaButti KM , Lapidus A , Lindquist EA , Lucas SM , Riley R , Salamov AA , Hoffmeister D , Schwenk D , Hadar Y , Yarden O , de Vries RP , Wiebenga A , Stenlid J , Eastwood D , Grigoriev IV , Berka RM , Blanchette RA , Kersten P , Martinez AT , Vicuna R , Cullen D
Ref : Proc Natl Acad Sci U S A , 109 :5458 , 2012
Abstract : Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium. Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium, respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn(2+). Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium.
ESTHER : Fernandez-Fueyo_2012_Proc.Natl.Acad.Sci.U.S.A_109_5458
PubMedSearch : Fernandez-Fueyo_2012_Proc.Natl.Acad.Sci.U.S.A_109_5458
PubMedID: 22434909
Gene_locus related to this paper: cers8-m2r3x2 , cers8-m2qf37 , cers8-m2pcy7 , cers8-m2pcz3 , cers8-m2qn26 , cers8-m2r654 , cers8-m2r8g9 , cers8-m2ps90 , cers8-m2qn44 , cers8-m2q837 , cers8-m2pjy6 , cers8-m2r609 , cers8-m2qy35 , cers8-m2r1n1 , cers8-m2rl22 , cers8-m2qkx5 , cers8-m2qib7 , cers8-m2rgs8 , cers8-m2rlx6 , cers8-m2r4p3 , cers8-m2rf62 , cers8-m2qyx5 , cers8-m2pcz2 , cers8-m2rm22 , cers8-m2qwb7 , cers8-m2r9u3 , cers8-m2pp23 , cers8-m2r613 , cers8-m2rup8 , cers8-m2piv7 , cers8-m2rch3 , cers8-m2qvf7 , cers8-m2qvb7 , cers8-m2qvb2 , cers8-m2pip7 , cers8-m2rb73 , cers8-m2qgd3 , cers8-m2rcg8 , cers8-m2rb68

Title : Insight into trade-off between wood decay and parasitism from the genome of a fungal forest pathogen - Olson_2012_New.Phytol_194_1001
Author(s) : Olson A , Aerts A , Asiegbu F , Belbahri L , Bouzid O , Broberg A , Canback B , Coutinho PM , Cullen D , Dalman K , Deflorio G , van Diepen LT , Dunand C , Duplessis S , Durling M , Gonthier P , Grimwood J , Fossdal CG , Hansson D , Henrissat B , Hietala A , Himmelstrand K , Hoffmeister D , Hogberg N , James TY , Karlsson M , Kohler A , Kues U , Lee YH , Lin YC , Lind M , Lindquist E , Lombard V , Lucas S , Lunden K , Morin E , Murat C , Park J , Raffaello T , Rouze P , Salamov A , Schmutz J , Solheim H , Stahlberg J , Velez H , de Vries RP , Wiebenga A , Woodward S , Yakovlev I , Garbelotto M , Martin F , Grigoriev IV , Stenlid J
Ref : New Phytol , 194 :1001 , 2012
Abstract : Parasitism and saprotrophic wood decay are two fungal strategies fundamental for succession and nutrient cycling in forest ecosystems. An opportunity to assess the trade-off between these strategies is provided by the forest pathogen and wood decayer Heterobasidion annosum sensu lato. We report the annotated genome sequence and transcript profiling, as well as the quantitative trait loci mapping, of one member of the species complex: H. irregulare. Quantitative trait loci critical for pathogenicity, and rich in transposable elements, orphan and secreted genes, were identified. A wide range of cellulose-degrading enzymes are expressed during wood decay. By contrast, pathogenic interaction between H. irregulare and pine engages fewer carbohydrate-active enzymes, but involves an increase in pectinolytic enzymes, transcription modules for oxidative stress and secondary metabolite production. Our results show a trade-off in terms of constrained carbohydrate decomposition and membrane transport capacity during interaction with living hosts. Our findings establish that saprotrophic wood decay and necrotrophic parasitism involve two distinct, yet overlapping, processes.
ESTHER : Olson_2012_New.Phytol_194_1001
PubMedSearch : Olson_2012_New.Phytol_194_1001
PubMedID: 22463738
Gene_locus related to this paper: 9homo-w4jrb9 , 9homo-w4jsg4 , 9homo-w4kds7 , 9homo-w4jwl9 , 9homo-w4kjy2 , 9homo-w4jw43 , 9homo-w4ka20 , 9homo-w4k8t3 , 9homo-w4jz43 , 9homo-w4k8q2 , 9homo-w4k910 , 9homo-w4k6f5 , 9homo-w4k6j3 , 9homo-w4k8n2 , 9homo-w4jrf3 , 9homo-w4ke07 , 9homo-w4k3i8 , 9homo-w4jqh1 , 9agam-w4k203 , 9agam-w4jpy3 , 9agam-w4jn81 , 9agam-w4jmz2

Title : Finished genome of the fungal wheat pathogen Mycosphaerella graminicola reveals dispensome structure, chromosome plasticity, and stealth pathogenesis - Goodwin_2011_PLoS.Genet_7_e1002070
Author(s) : Goodwin SB , M'Barek S B , Dhillon B , Wittenberg AH , Crane CF , Hane JK , Foster AJ , Van der Lee TA , Grimwood J , Aerts A , Antoniw J , Bailey A , Bluhm B , Bowler J , Bristow J , van der Burgt A , Canto-Canche B , Churchill AC , Conde-Ferraez L , Cools HJ , Coutinho PM , Csukai M , Dehal P , De Wit P , Donzelli B , van de Geest HC , van Ham RC , Hammond-Kosack KE , Henrissat B , Kilian A , Kobayashi AK , Koopmann E , Kourmpetis Y , Kuzniar A , Lindquist E , Lombard V , Maliepaard C , Martins N , Mehrabi R , Nap JP , Ponomarenko A , Rudd JJ , Salamov A , Schmutz J , Schouten HJ , Shapiro H , Stergiopoulos I , Torriani SF , Tu H , de Vries RP , Waalwijk C , Ware SB , Wiebenga A , Zwiers LH , Oliver RP , Grigoriev IV , Kema GH
Ref : PLoS Genet , 7 :e1002070 , 2011
Abstract : The plant-pathogenic fungus Mycosphaerella graminicola (asexual stage: Septoria tritici) causes septoria tritici blotch, a disease that greatly reduces the yield and quality of wheat. This disease is economically important in most wheat-growing areas worldwide and threatens global food production. Control of the disease has been hampered by a limited understanding of the genetic and biochemical bases of pathogenicity, including mechanisms of infection and of resistance in the host. Unlike most other plant pathogens, M. graminicola has a long latent period during which it evades host defenses. Although this type of stealth pathogenicity occurs commonly in Mycosphaerella and other Dothideomycetes, the largest class of plant-pathogenic fungi, its genetic basis is not known. To address this problem, the genome of M. graminicola was sequenced completely. The finished genome contains 21 chromosomes, eight of which could be lost with no visible effect on the fungus and thus are dispensable. This eight-chromosome dispensome is dynamic in field and progeny isolates, is different from the core genome in gene and repeat content, and appears to have originated by ancient horizontal transfer from an unknown donor. Synteny plots of the M. graminicola chromosomes versus those of the only other sequenced Dothideomycete, Stagonospora nodorum, revealed conservation of gene content but not order or orientation, suggesting a high rate of intra-chromosomal rearrangement in one or both species. This observed "mesosynteny" is very different from synteny seen between other organisms. A surprising feature of the M. graminicola genome compared to other sequenced plant pathogens was that it contained very few genes for enzymes that break down plant cell walls, which was more similar to endophytes than to pathogens. The stealth pathogenesis of M. graminicola probably involves degradation of proteins rather than carbohydrates to evade host defenses during the biotrophic stage of infection and may have evolved from endophytic ancestors.
ESTHER : Goodwin_2011_PLoS.Genet_7_e1002070
PubMedSearch : Goodwin_2011_PLoS.Genet_7_e1002070
PubMedID: 21695235
Gene_locus related to this paper: zymti-f9wzw8 , zymti-f9x2y6 , zymti-f9x423 , zymti-f9x813 , zymti-f9xa54 , zymti-f9xb42 , zymti-f9xbu5 , zymti-f9xcr9 , zymti-f9xdr7 , zymti-f9xer1 , zymti-f9xez8 , zymti-f9xfz9 , zymti-f9xh29 , zymti-f9xhe7 , zymti-f9xhr4 , zymti-f9xk09 , zymti-f9xns5 , zymti-f9xiu1 , zymti-f9xng3 , zymti-f9x4f2 , zymti-f9x4s7 , zymti-f9xdm8 , zymti-f9wwy9 , zymti-f9xkf2 , zymti-f9xlt3 , zymti-f9x0i3 , zymti-f9wwa6 , zymti-f9wyk7 , zymti-f9x3z1 , zymti-f9xf16 , zymtr-a0a1x7rhi5 , zymti-f9xfj3 , zymti-pks1

Title : Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea - Amselem_2011_PLoS.Genet_7_e1002230
Author(s) : Amselem J , Cuomo CA , van Kan JA , Viaud M , Benito EP , Couloux A , Coutinho PM , de Vries RP , Dyer PS , Fillinger S , Fournier E , Gout L , Hahn M , Kohn L , Lapalu N , Plummer KM , Pradier JM , Quevillon E , Sharon A , Simon A , ten Have A , Tudzynski B , Tudzynski P , Wincker P , Andrew M , Anthouard V , Beever RE , Beffa R , Benoit I , Bouzid O , Brault B , Chen Z , Choquer M , Collemare J , Cotton P , Danchin EG , Da Silva C , Gautier A , Giraud C , Giraud T , Gonzalez C , Grossetete S , Guldener U , Henrissat B , Howlett BJ , Kodira C , Kretschmer M , Lappartient A , Leroch M , Levis C , Mauceli E , Neuveglise C , Oeser B , Pearson M , Poulain J , Poussereau N , Quesneville H , Rascle C , Schumacher J , Segurens B , Sexton A , Silva E , Sirven C , Soanes DM , Talbot NJ , Templeton M , Yandava C , Yarden O , Zeng Q , Rollins JA , Lebrun MH , Dickman M
Ref : PLoS Genet , 7 :e1002230 , 2011
Abstract : Sclerotinia sclerotiorum and Botrytis cinerea are closely related necrotrophic plant pathogenic fungi notable for their wide host ranges and environmental persistence. These attributes have made these species models for understanding the complexity of necrotrophic, broad host-range pathogenicity. Despite their similarities, the two species differ in mating behaviour and the ability to produce asexual spores. We have sequenced the genomes of one strain of S. sclerotiorum and two strains of B. cinerea. The comparative analysis of these genomes relative to one another and to other sequenced fungal genomes is provided here. Their 38-39 Mb genomes include 11,860-14,270 predicted genes, which share 83% amino acid identity on average between the two species. We have mapped the S. sclerotiorum assembly to 16 chromosomes and found large-scale co-linearity with the B. cinerea genomes. Seven percent of the S. sclerotiorum genome comprises transposable elements compared to <1% of B. cinerea. The arsenal of genes associated with necrotrophic processes is similar between the species, including genes involved in plant cell wall degradation and oxalic acid production. Analysis of secondary metabolism gene clusters revealed an expansion in number and diversity of B. cinerea-specific secondary metabolites relative to S. sclerotiorum. The potential diversity in secondary metabolism might be involved in adaptation to specific ecological niches. Comparative genome analysis revealed the basis of differing sexual mating compatibility systems between S. sclerotiorum and B. cinerea. The organization of the mating-type loci differs, and their structures provide evidence for the evolution of heterothallism from homothallism. These data shed light on the evolutionary and mechanistic bases of the genetically complex traits of necrotrophic pathogenicity and sexual mating. This resource should facilitate the functional studies designed to better understand what makes these fungi such successful and persistent pathogens of agronomic crops.
ESTHER : Amselem_2011_PLoS.Genet_7_e1002230
PubMedSearch : Amselem_2011_PLoS.Genet_7_e1002230
PubMedID: 21876677
Gene_locus related to this paper: botci-cutas , botci-q6rki2 , botf4-g2y7k8 , botfb-dapb , botfu-g2xyd8 , botfu-g2ynh8 , scls1-a7e814 , scls1-a7edc9 , scls1-a7edh1 , scls1-a7emm0 , scls1-a7eti8 , scls1-a7eu48 , scls1-a7f208 , scls1-dapb , botf4-g2xqp7 , scls1-a7eqq8 , botf4-g2xqc6 , scls1-a7ebs4 , botf4-g2xn51 , scls1-a7f5m9 , botf4-g2xti4 , botf4-g2xtu7 , botf4-g2yfp1 , scls1-a7f534 , botf4-g2yys3 , scls1-a7erz9 , botf4-g2y037 , botf4-g2y0e1 , scls1-a7f706 , scls1-a7ewt6 , botf4-g2yuj6 , botf1-m7u3d1 , botf1-m7u430 , botf1-m7tei8 , botf1-m7u0w9 , botf1-m7tij6 , botf1-m7u819 , botf1-m7u6d8 , botf1-m7tzd4 , botf1-m7tqd7 , botf1-m7tyz9 , botf1-m7unl9 , botf1-m7u429 , botf1-m7u4s5 , botf1-m7ul92 , botf1-m7tx42 , botf1-m7u9h4 , botf1-m7u187 , botf1-m7uz64 , botf1-m7u4q4 , botf1-m7u2f6 , botf1-m7tt59 , botf1-m7v3h2 , botf1-m7u6c9 , botf1-m7tud9 , botf1-m7u309 , scls1-a7et87 , botf4-g2ylt4 , scls1-a7f5a0 , scls1-a7f900 , botf4-g2yib9 , scls1-a7f3m9 , scls1-a7er46 , botf4-g2y3y4 , botf4-g2xyy5 , botf1-m7uct5 , scls1-a7ea78 , scls1-kex1 , scls1-cbpya , botfb-cbpya , scls1-a7ecx1

Title : The plant cell wall-decomposing machinery underlies the functional diversity of forest fungi - Eastwood_2011_Science_333_762
Author(s) : Eastwood DC , Floudas D , Binder M , Majcherczyk A , Schneider P , Aerts A , Asiegbu FO , Baker SE , Barry K , Bendiksby M , Blumentritt M , Coutinho PM , Cullen D , de Vries RP , Gathman A , Goodell B , Henrissat B , Ihrmark K , Kauserud H , Kohler A , LaButti K , Lapidus A , Lavin JL , Lee YH , Lindquist E , Lilly W , Lucas S , Morin E , Murat C , Oguiza JA , Park J , Pisabarro AG , Riley R , Rosling A , Salamov A , Schmidt O , Schmutz J , Skrede I , Stenlid J , Wiebenga A , Xie X , Kues U , Hibbett DS , Hoffmeister D , Hogberg N , Martin F , Grigoriev IV , Watkinson SC
Ref : Science , 333 :762 , 2011
Abstract : Brown rot decay removes cellulose and hemicellulose from wood--residual lignin contributing up to 30% of forest soil carbon--and is derived from an ancestral white rot saprotrophy in which both lignin and cellulose are decomposed. Comparative and functional genomics of the "dry rot" fungus Serpula lacrymans, derived from forest ancestors, demonstrated that the evolution of both ectomycorrhizal biotrophy and brown rot saprotrophy were accompanied by reductions and losses in specific protein families, suggesting adaptation to an intercellular interaction with plant tissue. Transcriptome and proteome analysis also identified differences in wood decomposition in S. lacrymans relative to the brown rot Postia placenta. Furthermore, fungal nutritional mode diversification suggests that the boreal forest biome originated via genetic coevolution of above- and below-ground biota.
ESTHER : Eastwood_2011_Science_333_762
PubMedSearch : Eastwood_2011_Science_333_762
PubMedID: 21764756
Gene_locus related to this paper: serl3-f8prj2 , serl3-f8qcc4 , serl9-f8ngp6 , serl9-f8nhd7 , serl9-f8nhq9 , serl9-f8nq77 , serl9-f8nr67 , serl9-f8nrt5 , serl9-f8nvy7.1 , serl9-f8nvy7.2 , serl9-f8nvy8 , serl9-f8nxt0.1 , serl9-f8nxt0.2 , serl9-f8nzr3 , serl9-f8p0f0 , serl9-f8p6v0 , serl9-f8p015 , serl9-f8p018 , serl9-f8p386 , serl9-f8paz8 , serl9-f8pbv1 , serl9-f8pby1 , serl9-f8pc25 , serl9-f8pc39 , serl9-f8nia7 , serl3-f8pju2 , serl9-f8peh1 , serl9-nps3

Title : Comparative genomic analysis of the thermophilic biomass-degrading fungi Myceliophthora thermophila and Thielavia terrestris - Berka_2011_Nat.Biotechnol_29_922
Author(s) : Berka RM , Grigoriev IV , Otillar R , Salamov A , Grimwood J , Reid I , Ishmael N , John T , Darmond C , Moisan MC , Henrissat B , Coutinho PM , Lombard V , Natvig DO , Lindquist E , Schmutz J , Lucas S , Harris P , Powlowski J , Bellemare A , Taylor D , Butler G , de Vries RP , Allijn IE , van den Brink J , Ushinsky S , Storms R , Powell AJ , Paulsen IT , Elbourne LD , Baker SE , Magnuson J , Laboissiere S , Clutterbuck AJ , Martinez D , Wogulis M , de Leon AL , Rey MW , Tsang A
Ref : Nat Biotechnol , 29 :922 , 2011
Abstract : Thermostable enzymes and thermophilic cell factories may afford economic advantages in the production of many chemicals and biomass-based fuels. Here we describe and compare the genomes of two thermophilic fungi, Myceliophthora thermophila and Thielavia terrestris. To our knowledge, these genomes are the first described for thermophilic eukaryotes and the first complete telomere-to-telomere genomes for filamentous fungi. Genome analyses and experimental data suggest that both thermophiles are capable of hydrolyzing all major polysaccharides found in biomass. Examination of transcriptome data and secreted proteins suggests that the two fungi use shared approaches in the hydrolysis of cellulose and xylan but distinct mechanisms in pectin degradation. Characterization of the biomass-hydrolyzing activity of recombinant enzymes suggests that these organisms are highly efficient in biomass decomposition at both moderate and high temperatures. Furthermore, we present evidence suggesting that aside from representing a potential reservoir of thermostable enzymes, thermophilic fungi are amenable to manipulation using classical and molecular genetics.
ESTHER : Berka_2011_Nat.Biotechnol_29_922
PubMedSearch : Berka_2011_Nat.Biotechnol_29_922
PubMedID: 21964414
Gene_locus related to this paper: thiha-cip2 , thite-g2r8b5 , thite-g2rcm8 , thite-g2r192 , thiha-g2qdy2 , thiha-g2qh51 , thite-g2rae6 , thite-g2r5h0 , thiha-g2qj94 , thiha-g2qnb2 , thite-g2rg14 , myctt-g2q973 , thite-g2qtu3 , myctt-g2qpr0 , thite-g2rhm0 , 9pezi-a0a3s4b069 , myctt-g2qmb4 , thett-g2qur2

Title : Genome sequence of the model mushroom Schizophyllum commune - Ohm_2010_Nat.Biotechnol_28_957
Author(s) : Ohm RA , de Jong JF , Lugones LG , Aerts A , Kothe E , Stajich JE , de Vries RP , Record E , Levasseur A , Baker SE , Bartholomew KA , Coutinho PM , Erdmann S , Fowler TJ , Gathman AC , Lombard V , Henrissat B , Knabe N , Kues U , Lilly WW , Lindquist E , Lucas S , Magnuson JK , Piumi F , Raudaskoski M , Salamov A , Schmutz J , Schwarze FW , vanKuyk PA , Horton JS , Grigoriev IV , Wosten HA
Ref : Nat Biotechnol , 28 :957 , 2010
Abstract : Much remains to be learned about the biology of mushroom-forming fungi, which are an important source of food, secondary metabolites and industrial enzymes. The wood-degrading fungus Schizophyllum commune is both a genetically tractable model for studying mushroom development and a likely source of enzymes capable of efficient degradation of lignocellulosic biomass. Comparative analyses of its 38.5-megabase genome, which encodes 13,210 predicted genes, reveal the species's unique wood-degrading machinery. One-third of the 471 genes predicted to encode transcription factors are differentially expressed during sexual development of S. commune. Whereas inactivation of one of these, fst4, prevented mushroom formation, inactivation of another, fst3, resulted in more, albeit smaller, mushrooms than in the wild-type fungus. Antisense transcripts may also have a role in the formation of fruiting bodies. Better insight into the mechanisms underlying mushroom formation should affect commercial production of mushrooms and their industrial use for producing enzymes and pharmaceuticals.
ESTHER : Ohm_2010_Nat.Biotechnol_28_957
PubMedSearch : Ohm_2010_Nat.Biotechnol_28_957
PubMedID: 20622885
Gene_locus related to this paper: schcm-d8pqz6 , schcm-d8prj2 , schcm-d8pug6 , schcm-d8pxe8 , schcm-d8pxe9 , schcm-d8pxz1 , schcm-d8q1c7 , schcm-d8q2b4 , schcm-d8q3j1 , schcm-d8q5m5 , schcm-d8q7x7.1 , schcm-d8q7x7.2 , schcm-d8q8y8 , schcm-d8q9n6 , schcm-d8q697 , schcm-d8qip8 , schcm-d8q5s5 , schcm-d8ppb3 , schcm-d8ppb6 , schcm-d8pv73 , schcm-d8pzm1 , schcm-d8q5a7 , schcm-d8qif0

Title : Two glucuronoyl esterases of Phanerochaete chrysosporium - Duranova_2009_Arch.Microbiol_191_133
Author(s) : Duranova M , Spanikova S , Wosten HA , Biely P , de Vries RP
Ref : Arch Microbiol , 191 :133 , 2009
Abstract : The white-rot fungus Phanerochaete chrysosporium produces glucuronoyl esterase, a recently discovered carbohydrate esterase, during growth on sugar beet pulp. Two putative genes encoding this enzyme, ge1 and ge2, were isolated and cloned. Heterologous expression in Aspergillus vadensis, Pycnoporus cinnabarinus and Schizophyllum commune resulted in extracellular glucuronoyl esterase activity, demonstrating that these genes encode this enzymatic function. The amino acid sequence of GE1 was used to identify homologous genes in the genomes of twenty-four fungi. Approximately half of the genomes, both from ascomycetes and basidiomycetes, contained putative orthologues, but their presence could not be assigned to any of fungal class or subclass. Comparison of the amino acid sequences of identified and putative glucuronoyl esterases to other types of carbohydrate esterases (CE) confirmed that they form a separate family of CEs. These enzymes are interesting candidates for biotechnological applications such as the separation of lignin and hemicellulose.
ESTHER : Duranova_2009_Arch.Microbiol_191_133
PubMedSearch : Duranova_2009_Arch.Microbiol_191_133
PubMedID: 18854978
Gene_locus related to this paper: wolco-gce1 , phacr-gce1

Title : The 2008 update of the Aspergillus nidulans genome annotation: a community effort - Wortman_2009_Fungal.Genet.Biol_46 Suppl 1_S2
Author(s) : Wortman JR , Gilsenan JM , Joardar V , Deegan J , Clutterbuck J , Andersen MR , Archer D , Bencina M , Braus G , Coutinho P , von Dohren H , Doonan J , Driessen AJ , Durek P , Espeso E , Fekete E , Flipphi M , Estrada CG , Geysens S , Goldman G , de Groot PW , Hansen K , Harris SD , Heinekamp T , Helmstaedt K , Henrissat B , Hofmann G , Homan T , Horio T , Horiuchi H , James S , Jones M , Karaffa L , Karanyi Z , Kato M , Keller N , Kelly DE , Kiel JA , Kim JM , van der Klei IJ , Klis FM , Kovalchuk A , Krasevec N , Kubicek CP , Liu B , Maccabe A , Meyer V , Mirabito P , Miskei M , Mos M , Mullins J , Nelson DR , Nielsen J , Oakley BR , Osmani SA , Pakula T , Paszewski A , Paulsen I , Pilsyk S , Pocsi I , Punt PJ , Ram AF , Ren Q , Robellet X , Robson G , Seiboth B , van Solingen P , Specht T , Sun J , Taheri-Talesh N , Takeshita N , Ussery D , vanKuyk PA , Visser H , van de Vondervoort PJ , de Vries RP , Walton J , Xiang X , Xiong Y , Zeng AP , Brandt BW , Cornell MJ , van den Hondel CA , Visser J , Oliver SG , Turner G
Ref : Fungal Genet Biol , 46 Suppl 1 :S2 , 2009
Abstract : The identification and annotation of protein-coding genes is one of the primary goals of whole-genome sequencing projects, and the accuracy of predicting the primary protein products of gene expression is vital to the interpretation of the available data and the design of downstream functional applications. Nevertheless, the comprehensive annotation of eukaryotic genomes remains a considerable challenge. Many genomes submitted to public databases, including those of major model organisms, contain significant numbers of wrong and incomplete gene predictions. We present a community-based reannotation of the Aspergillus nidulans genome with the primary goal of increasing the number and quality of protein functional assignments through the careful review of experts in the field of fungal biology.
ESTHER : Wortman_2009_Fungal.Genet.Biol_46 Suppl 1_S2
PubMedSearch : Wortman_2009_Fungal.Genet.Biol_46 Suppl 1_S2
PubMedID: 19146970
Gene_locus related to this paper: emeni-axe1 , emeni-c8v4m7 , emeni-faec , emeni-ppme1 , emeni-q5ara9 , emeni-q5arf0 , emeni-q5as30 , emeni-q5ase8 , emeni-q5av79 , emeni-q5aw09 , emeni-q5awc3 , emeni-q5awc7 , emeni-q5awu9 , emeni-q5aww4 , emeni-q5ax50 , emeni-q5ay37 , emeni-q5ay57 , emeni-q5ay59 , emeni-q5ayk9 , emeni-q5ays5 , emeni-q5az32 , emeni-q5az91 , emeni-q5az97 , emeni-q5azp1 , emeni-q5b0i6 , emeni-q5b1h2 , emeni-q5b2a9 , emeni-q5b2p7 , emeni-q5b3d2 , emeni-q5b4q7 , emeni-q5b5u7 , emeni-q5b5y4 , emeni-q5b9e7 , emeni-q5b9i0 , emeni-q5b364 , emeni-q5b446 , emeni-q5b938 , emeni-q5ba78 , emeni-q5bcd1 , emeni-q5bcd2 , emeni-q5bde7 , emeni-q5bdr0 , emeni-q5bf92 , emeni-q7si80 , emeni-q5bdv9 , emeni-c8vu15 , 9euro-a0a3d8t644 , emeni-q5b719 , emeni-q5ax97 , emeni-tdia , emeni-afoc , emeni-dbae

Title : The genome sequence of the model ascomycete fungus Podospora anserina - Espagne_2008_Genome.Biol_9_R77
Author(s) : Espagne E , Lespinet O , Malagnac F , Da Silva C , Jaillon O , Porcel BM , Couloux A , Aury JM , Segurens B , Poulain J , Anthouard V , Grossetete S , Khalili H , Coppin E , Dequard-Chablat M , Picard M , Contamine V , Arnaise S , Bourdais A , Berteaux-Lecellier V , Gautheret D , de Vries RP , Battaglia E , Coutinho PM , Danchin EG , Henrissat B , Khoury RE , Sainsard-Chanet A , Boivin A , Pinan-Lucarre B , Sellem CH , Debuchy R , Wincker P , Weissenbach J , Silar P
Ref : Genome Biol , 9 :R77 , 2008
Abstract : BACKGROUND: The dung-inhabiting ascomycete fungus Podospora anserina is a model used to study various aspects of eukaryotic and fungal biology, such as ageing, prions and sexual development. RESULTS: We present a 10X draft sequence of P. anserina genome, linked to the sequences of a large expressed sequence tag collection. Similar to higher eukaryotes, the P. anserina transcription/splicing machinery generates numerous non-conventional transcripts. Comparison of the P. anserina genome and orthologous gene set with the one of its close relatives, Neurospora crassa, shows that synteny is poorly conserved, the main result of evolution being gene shuffling in the same chromosome. The P. anserina genome contains fewer repeated sequences and has evolved new genes by duplication since its separation from N. crassa, despite the presence of the repeat induced point mutation mechanism that mutates duplicated sequences. We also provide evidence that frequent gene loss took place in the lineages leading to P. anserina and N. crassa. P. anserina contains a large and highly specialized set of genes involved in utilization of natural carbon sources commonly found in its natural biotope. It includes genes potentially involved in lignin degradation and efficient cellulose breakdown. CONCLUSION: The features of the P. anserina genome indicate a highly dynamic evolution since the divergence of P. anserina and N. crassa, leading to the ability of the former to use specific complex carbon sources that match its needs in its natural biotope.
ESTHER : Espagne_2008_Genome.Biol_9_R77
PubMedSearch : Espagne_2008_Genome.Biol_9_R77
PubMedID: 18460219
Gene_locus related to this paper: podan-b2a8u1 , podan-b2a9c4 , podan-b2a9k6 , podan-b2aa90 , podan-b2ab33 , podan-b2abs0 , podan-b2ac17 , podan-b2ack2 , podan-b2ad07 , podan-b2adj6 , podan-b2adk0 , podan-b2ae59 , podan-b2aee7 , podan-b2af51 , podan-b2afn5 , podan-b2afu6 , podan-b2akq7 , podan-b2aly0 , podan-b2am11 , podan-b2an24 , podan-b2ank1 , podan-b2apa8 , podan-b2api8 , podan-b2apj6 , podan-b2arl9 , podan-b2arz7 , podan-b2ase4 , podan-b2atn0 , podan-b2au46 , podan-b2aun9 , podan-b2av47 , podan-b2ava6 , podan-b2avm3 , podan-b2avu5 , podan-b2avx3 , podan-b2awk8 , podan-b2axk2 , podan-b2axz2 , podan-b2b1p7 , podan-b2b5e4 , podan-b2b6n7 , podan-b2b069 , podan-b2b073 , podan-b2b395 , podan-dapb , podan-b2afr0 , podan-b2a9k8 , podan-b2atb3 , podan-b2aca3 , podan-b2arv3 , podan-b2ank5 , podan-b2ax54 , podan-b2ad56 , podan-b2anm1 , podan-b2aya1 , podan-b2b164 , podan-a0a090d4h4 , podan-a0a090ccl8 , podan-b2b5p4 , podan-b2azp1 , podan-b2af75 , podan-b2alm5 , podan-b2ass5 , podan-b2aez8 , podan-kex1 , podan-cbpya

Title : Biotechnological applications and potential of fungal feruloyl esterases based on prevalence, classification and biochemical diversity - Benoit_2008_Biotechnol.Lett_30_387
Author(s) : Benoit I , Danchin EG , Bleichrodt RJ , de Vries RP
Ref : Biotechnol Lett , 30 :387 , 2008
Abstract : Feruloyl esterases are part of the enzymatic spectrum employed by fungi and other microorganisms to degrade plant polysaccharides. They release ferulic acid and other aromatic acids from these polymeric structures and have received an increasing interest in industrial applications such as in the food, pulp and paper and bio-fuel industries. This review provides an overview of the current knowledge on fungal feruloyl esterases focussing in particular on the differences in substrate specificity, regulation of their production, prevalence of these enzymes in fungal genomes and industrial applications.
ESTHER : Benoit_2008_Biotechnol.Lett_30_387
PubMedSearch : Benoit_2008_Biotechnol.Lett_30_387
PubMedID: 17973091

Title : Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88 - Pel_2007_Nat.Biotechnol_25_221
Author(s) : Pel HJ , de Winde JH , Archer DB , Dyer PS , Hofmann G , Schaap PJ , Turner G , de Vries RP , Albang R , Albermann K , Andersen MR , Bendtsen JD , Benen JA , van den Berg M , Breestraat S , Caddick MX , Contreras R , Cornell M , Coutinho PM , Danchin EG , Debets AJ , Dekker P , van Dijck PW , van Dijk A , Dijkhuizen L , Driessen AJ , d'Enfert C , Geysens S , Goosen C , Groot GS , de Groot PW , Guillemette T , Henrissat B , Herweijer M , van den Hombergh JP , van den Hondel CA , van der Heijden RT , van der Kaaij RM , Klis FM , Kools HJ , Kubicek CP , van Kuyk PA , Lauber J , Lu X , van der Maarel MJ , Meulenberg R , Menke H , Mortimer MA , Nielsen J , Oliver SG , Olsthoorn M , Pal K , van Peij NN , Ram AF , Rinas U , Roubos JA , Sagt CM , Schmoll M , Sun J , Ussery D , Varga J , Vervecken W , van de Vondervoort PJ , Wedler H , Wosten HA , Zeng AP , van Ooyen AJ , Visser J , Stam H
Ref : Nat Biotechnol , 25 :221 , 2007
Abstract : The filamentous fungus Aspergillus niger is widely exploited by the fermentation industry for the production of enzymes and organic acids, particularly citric acid. We sequenced the 33.9-megabase genome of A. niger CBS 513.88, the ancestor of currently used enzyme production strains. A high level of synteny was observed with other aspergilli sequenced. Strong function predictions were made for 6,506 of the 14,165 open reading frames identified. A detailed description of the components of the protein secretion pathway was made and striking differences in the hydrolytic enzyme spectra of aspergilli were observed. A reconstructed metabolic network comprising 1,069 unique reactions illustrates the versatile metabolism of A. niger. Noteworthy is the large number of major facilitator superfamily transporters and fungal zinc binuclear cluster transcription factors, and the presence of putative gene clusters for fumonisin and ochratoxin A synthesis.
ESTHER : Pel_2007_Nat.Biotechnol_25_221
PubMedSearch : Pel_2007_Nat.Biotechnol_25_221
PubMedID: 17259976
Gene_locus related to this paper: aspna-g3yal2 , aspnc-a2q8r7 , aspnc-a2q814 , aspnc-a2qb93 , aspnc-a2qbd3 , aspnc-a2qbh3 , aspnc-a2qbx7 , aspnc-a2qdj6 , aspnc-a2qe77 , aspnc-a2qf54 , aspnc-a2qfe9 , aspnc-a2qg33 , aspnc-a2qgj6 , aspnc-a2qgm6 , aspnc-a2qh52 , aspnc-a2qh76 , aspnc-a2qh85 , aspnc-a2qhe2 , aspnc-a2qi32 , aspnc-a2qib2 , aspnc-a2qk14 , aspnc-a2ql23 , aspnc-a2ql89 , aspnc-a2ql90 , aspnc-a2qla0 , aspnc-a2qlz0 , aspnc-a2qm14 , aspnc-a2qmk5 , aspnc-a2qms0 , aspnc-a2qn29 , aspnc-a2qn56 , aspnc-a2qn70 , aspnc-a2qnw9 , aspnc-a2qr21 , aspnc-a2qs22 , aspnc-a2qt50 , aspnc-a2qti9 , aspnc-a2qtz0 , aspnc-a2quc1 , aspnc-a2qw06 , aspnc-a2qwz6 , aspnc-a2qx92 , aspnc-a2qyf0 , aspnc-a2qys7 , aspnc-a2qz72 , aspnc-a2qzn6 , aspnc-a2qzr0 , aspnc-a2qzs1 , aspnc-a2qzx0 , aspnc-a2qzx4 , aspnc-a2r0p4 , aspnc-a2r0u0 , aspnc-a2r1p3 , aspnc-a2r1r5 , aspnc-a2r2i5 , aspnc-a2r2l0 , aspnc-a2r3s8 , aspnc-a2r4c0 , aspnc-a2r4j8 , aspnc-a2r5r4 , aspnc-a2r6g3 , aspnc-a2r6h5 , aspnc-a2r6h8 , aspnc-a2r7q1 , aspnc-a2r8r3 , aspnc-a2r8z3 , aspnc-a2r9y8 , aspnc-a2r032 , aspnc-a2r040 , aspnc-a2r273 , aspnc-a2r496 , aspnc-a2r502 , aspnc-a2ra07 , aspnc-a2rap4 , aspnc-a2raq2 , aspnc-a2rav1 , aspnc-a5aaf4 , aspnc-a5ab63 , aspnc-a5abc6 , aspnc-a5abe5 , aspnc-a5abe8 , aspnc-a5abf0 , aspnc-a5abh9 , aspnc-a5abk1 , aspnc-a5abt2 , aspnc-a5abz1 , aspnc-atg15 , aspnc-axe1 , aspnc-cuti1 , aspnc-cuti2 , aspnc-faec , aspng-a2q8w0 , aspng-a2qs46 , aspng-a2qst4 , aspng-a2qv27 , aspng-a2qzk9 , aspng-a2r0p8 , aspng-a2r225 , aspng-DAPB , aspng-DPP5 , aspng-faeb , aspni-APSC , aspni-EstA , aspni-FAEA , aspni-PAPA , aspkw-g7y0v7 , aspnc-a2qt47 , aspnc-a2qt66 , aspnc-a2r199 , aspnc-a2r871 , aspnc-a2qbp6 , aspnc-a2qqa1 , aspnc-a2qt70 , aspna-g3y5a6 , aspna-g3xpw9 , aspnc-a2qw57 , aspaw-a0a401kcz4 , aspna-alba , aspnc-kex1 , aspnc-cbpya , aspnc-a2qbg8

Title : Identification of genes encoding microbial glucuronoyl esterases - Li_2007_FEBS.Lett_581_4029
Author(s) : Li XL , Spanikova S , de Vries RP , Biely P
Ref : FEBS Letters , 581 :4029 , 2007
Abstract : One type of covalent linkages connecting lignin and hemicellulose in plant cell walls is the ester linkage between 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols. An enzyme that could hydrolyze such linkages, named glucuronoyl esterase, occurs in the cellulolytic system of the wood-rotting fungus Schizophyllum commune. Here we report partial amino acid sequences of the enzyme and the results of subsequent search for homologous genes in sequenced genomes. The homologous genes of unknown functions were found in genomes of several filamentous fungi and one bacterium. The gene corresponding to the cip2 gene of Hypocrea jecorina (Trichoderma reesei), known to be up-regulated under conditions of induction of cellulolytic and hemicellulolytic enzymes, was over-expressed in H. jecorina. The product of the cip2 gene was purified to homogeneity and shown to exhibit glucuronoyl esterase activity.
ESTHER : Li_2007_FEBS.Lett_581_4029
PubMedSearch : Li_2007_FEBS.Lett_581_4029
PubMedID: 17678650
Gene_locus related to this paper: hypjq-cip2

Title : Regulation of Aspergillus genes encoding plant cell wall polysaccharide-degrading enzymes\; relevance for industrial production - de Vries_2003_Appl.Microbiol.Biotechnol_61_10
Author(s) : de Vries RP
Ref : Applied Microbiology & Biotechnology , 61 :10 , 2003
Abstract : The genus Aspergillus is widely used for the production of plant cell wall polysaccharide-degrading enzymes. The range of enzymes purified from these fungi covers nearly every function required for the complete degradation of cellulose, xyloglucan, xylan, galacto(gluco)mannan and pectin. This paper describes the Aspergillus enzymes involved in the degradation of these polysaccharides and discusses the regulatory systems involved in the expression of the genes encoding these proteins. The latter is of major importance in the large-scale production of these enzymes for industrial applications.
ESTHER : de Vries_2003_Appl.Microbiol.Biotechnol_61_10
PubMedSearch : de Vries_2003_Appl.Microbiol.Biotechnol_61_10
PubMedID: 12658510

Title : Glycerol dehydrogenase, encoded by gldB is essential for osmotolerance in Aspergillus nidulans - de Vries_2003_Mol.Microbiol_49_131
Author(s) : de Vries RP , Flitter SJ , van de Vondervoort PJ , Chaveroche MK , Fontaine T , Fillinger S , Ruijter GJ , d'Enfert C , Visser J
Ref : Molecular Microbiology , 49 :131 , 2003
Abstract : We have characterized the Aspergillus nidulans gldB gene encoding a NADP+-dependent glycerol dehydrogenase. A basal expression level was observed for gldB, which increased significantly under conditions of hyper-osmotic shock (1 M NaCl). Growth of strains in which gldB was disrupted was severely reduced on plates containing 1% glucose and 1 M NaCl, but these strains were able to grow on plates containing 1 M NaCl and 1% glycerol, arabitol, mannitol or erythritol. Uptake of these polyols compensated for the inability of the gldB disruptants to produce glycerol. Presence of 1% glucose in these plates prevented growth restoration by all the polyols tested with the exemption of glycerol, indicating that uptake of mannitol, arabitol and erythritol is subject to glucose repression, whereas uptake of glycerol is significantly less or not repressed. No intracellular glycerol dehydrogenase activity could be detected in the gldB disruption strains. Intracellular glycerol levels in these strains were strongly decreased compared to wild type, whereas intracellular mannitol, erythritol and arabitol levels were increased. Conidia of the gldB disruption strain did not accumulate glycerol upon germination in glucose media with or without 1 M NaCl and germ tube emergence was significantly delayed in this strain in the presence of 1 M NaCl in comparison to the wild type. These data indicate that gldB is essential for osmotolerance in A. nidulans and that the pathways for glycerol biosynthesis under osmotic stress differ between yeast and filamentous fungi.
ESTHER : de Vries_2003_Mol.Microbiol_49_131
PubMedSearch : de Vries_2003_Mol.Microbiol_49_131
PubMedID: 12823816

Title : Mannitol is required for stress tolerance in Aspergillus niger conidiospores - Ruijter_2003_Eukaryot.Cell_2_690
Author(s) : Ruijter GJ , Bax M , Patel H , Flitter SJ , van de Vondervoort PJ , de Vries RP , vanKuyk PA , Visser J
Ref : Eukaryot Cell , 2 :690 , 2003
Abstract : D-Mannitol is the predominant carbon compound in conidiospores of the filamentous fungus Aspergillus niger and makes up 10 to 15% of the dry weight. A number of physiological functions have been ascribed to mannitol, including serving as a reserve carbon source, as an antioxidant, and to store reducing power. In this study, we cloned and characterized the A. niger mpdA gene, which encodes mannitol 1-phosphate dehydrogenase (MPD), the first enzyme in the mannitol biosynthesis pathway. The mpdA promoter contains putative binding sites for the development-specific transcription factors BRLA and ABAA. Furthermore, increased expression of mpdA in sporulating mycelium suggests that mannitol biosynthesis is, to a certain extent, developmentally regulated in A. niger. Inactivation of mpdA abolished mannitol biosynthesis in growing mycelium and reduced the mannitol level in conidiospores to 30% that in the wild type, indicating that MPD and mannitol 1-phosphate phosphatase form the major metabolic pathway for mannitol biosynthesis in A. niger. The viability of spores after prolonged storage and germination kinetics were normal in an mpdA null mutant, indicating that mannitol does not play an essential role as a reserve carbon source in A. niger conidia. However, conidiospores of a DeltampdA strain were extremely sensitive to a variety of stress conditions, including high temperature, oxidative stress and, to a lesser extent, freezing and lyophilization. Since mannitol supplied in the medium during sporulation repaired this deficiency, mannitol appears to be essential for the protection of A. niger spores against cell damage under these stress conditions.
ESTHER : Ruijter_2003_Eukaryot.Cell_2_690
PubMedSearch : Ruijter_2003_Eukaryot.Cell_2_690
PubMedID: 12912888

Title : Isolation and characterization of two specific regulatory Aspergillus niger mutants shows antagonistic regulation of arabinan and xylan metabolism - de Groot_2003_Microbiology_149_1183
Author(s) : de Groot MJ , van de Vondervoort PJ , de Vries RP , vanKuyk PA , Ruijter GJ , Visser J
Ref : Microbiology , 149 :1183 , 2003
Abstract : This paper describes two Aspergillus niger mutants (araA and araB) specifically disturbed in the regulation of the arabinanase system in response to the presence of L-arabinose. Expression of the three known L-arabinose-induced arabinanolytic genes, abfA, abfB and abnA, was substantially decreased or absent in the araA and araB strains compared to the wild-type when incubated in the presence of L-arabinose or L-arabitol. In addition, the intracellular activities of L-arabitol dehydrogenase and L-arabinose reductase, involved in L-arabinose catabolism, were decreased in the araA and araB strains. Finally, the data show that the gene encoding D-xylulose kinase, xkiA, is also under control of the arabinanolytic regulatory system. L-Arabitol, most likely the true inducer of the arabinanolytic and L-arabinose catabolic genes, accumulated to a high intracellular concentration in the araA and araB mutants. This indicates that the decrease of expression of the arabinanolytic genes was not due to lack of inducer accumulation. Therefore, it is proposed that the araA and araB mutations are localized in positive-acting components of the regulatory system involved in the expression of the arabinanase-encoding genes and the genes encoding the L-arabinose catabolic pathway.
ESTHER : de Groot_2003_Microbiology_149_1183
PubMedSearch : de Groot_2003_Microbiology_149_1183
PubMedID: 12724380

Title : Expression profiling of pectinolytic genes from Aspergillus niger - de Vries_2002_FEBS.Lett_530_41
Author(s) : de Vries RP , Jansen J , Aguilar G , Parenicova L , Joosten V , Wulfert F , Benen JA , Visser J
Ref : FEBS Letters , 530 :41 , 2002
Abstract : The expression of 26 pectinolytic genes from Aspergillus niger was studied in a wild type strain and a CreA derepressed strain, under 16 different growth conditions, to obtain an expression profile for each gene. These expression profiles were then submitted to cluster analysis to identify subsets of genes with similar expression profiles. With the exception of the feruloyl esterase encoding genes, all genes were expressed in the presence of D-galacturonic acid, polygalacturonate, and/or sugar beet pectin. Despite this general observation five distinct groups of genes were identified. The major group consisted of 12 genes of which the corresponding enzymes act on the pectin backbone and for which the expression, in general, is higher after 8 and 24 h of incubation, than after 2 or 4 h. Two other groups of genes encoding pectin main chain acting enzymes were detected. Two additional groups contained genes encoding L-arabinose and D-galactose releasing enzymes, and ferulic acid releasing enzymes, respectively. The genes encoding beta-galactosidase and the L-arabinose releasing enzymes were not only expressed in the presence of D-galacturonic acid, but also in the presence of L-arabinose, suggesting that they are under the control of two regulatory systems. Similarly, the rhamnogalacturonan acetylesterase encoding gene was not only expressed in the presence of D-galacturonic acid, polygalacturonate and sugar beet pectin, but also in the presence of L-rhamnose. The data presented provides indications for a general pectinolytic regulatory system responding to D-galacturonic acid or a metabolite derived from it. In addition, subsets of pectinolytic genes are expressed in response to the presence of L-arabinose, L-rhamnose or ferulic acid.
ESTHER : de Vries_2002_FEBS.Lett_530_41
PubMedSearch : de Vries_2002_FEBS.Lett_530_41
PubMedID: 12387863

Title : The beta-1,4-endogalactanase A gene from Aspergillus niger is specifically induced on arabinose and galacturonic acid and plays an important role in the degradation of pectic hairy regions - De Vries_2002_Eur.J.Biochem_269_4985
Author(s) : de Vries RP , Parenicova L , Hinz SW , Kester HC , Beldman G , Benen JA , Visser J
Ref : European Journal of Biochemistry , 269 :4985 , 2002
Abstract : The Aspergillus nigerbeta-1,4-endogalactanase encoding gene (galA) was cloned and characterized. The expression of galA in A. niger was only detected in the presence of sugar beet pectin, d-galacturonic acid and l-arabinose, suggesting that galA is coregulated with both the pectinolytic genes as well as the arabinanolytic genes. The corresponding enzyme, endogalactanase A (GALA), contains both active site residues identified previously for the Pseudomonas fluorescensbeta-1,4-endogalactanase. The galA gene was overexpressed to facilitate purification of GALA. The enzyme has a molecular mass of 48.5 kDa and a pH optimum between 4 and 4.5. Incubations of arabinogalactans of potato, onion and soy with GALA resulted initially in the release of d-galactotriose and d-galactotetraose, whereas prolonged incubation resulted in d-galactose and d-galactobiose, predominantly. MALDI-TOF analysis revealed the release of l-arabinose substituted d-galacto-oligosaccharides from soy arabinogalactan. This is the first report of the ability of a beta-1,4-endogalactanase to release substituted d-galacto-oligosaccharides. GALA was not active towards d-galacto-oligosaccharides that were substituted with d-glucose at the reducing end.
ESTHER : De Vries_2002_Eur.J.Biochem_269_4985
PubMedSearch : De Vries_2002_Eur.J.Biochem_269_4985
PubMedID: 12383257

Title : Regulation of the alpha-glucuronidase-encoding gene ( aguA) from Aspergillus niger - de Vries_2002_Mol.Genet.Genomics_268_96
Author(s) : de Vries RP , van de Vondervoort PJ , Hendriks L , van de Belt M , Visser J
Ref : Mol Genet Genomics , 268 :96 , 2002
Abstract : The alpha-glucuronidase gene aguA from Aspergillus niger was cloned and characterised. Analysis of the promoter region of aguA revealed the presence of four putative binding sites for the major carbon catabolite repressor protein CREA and one putative binding site for the transcriptional activator XLNR. In addition, a sequence motif was detected which differed only in the last nucleotide from the XLNR consensus site. A construct in which part of the aguA coding region was deleted still resulted in production of a stable mRNA upon transformation of A. niger. The putative XLNR binding sites and two of the putative CREA binding sites were mutated individually in this construct and the effects on expression were examined in A. niger transformants. Northern analysis of the transformants revealed that the consensus XLNR site is not actually functional in the aguA promoter, whereas the sequence that diverges from the consensus at a single position is functional. This indicates that XLNR is also able to bind to the sequence GGCTAG, and the XLNR binding site consensus should therefore be changed to GGCTAR. Both CREA sites are functional, indicating that CREA has a strong influence on aguA expression. A detailed expression analysis of aguA in four genetic backgrounds revealed a second regulatory system involved in activation of aguA gene expression. This system responds to the presence of glucuronic and galacturonic acids, and is not dependent on XLNR.
ESTHER : de Vries_2002_Mol.Genet.Genomics_268_96
PubMedSearch : de Vries_2002_Mol.Genet.Genomics_268_96
PubMedID: 12242504

Title : The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds - de Vries_2002_Biochem.J_363_377
Author(s) : de Vries RP , vanKuyk PA , Kester HC , Visser J
Ref : Biochemical Journal , 363 :377 , 2002
Abstract : The faeB gene encoding a second feruloyl esterase from Aspergillus niger has been cloned and characterized. It consists of an open reading frame of 1644 bp containing one intron. The gene encodes a protein of 521 amino acids that has sequence similarity to that of an Aspergillus oryzae tannase. However, the encoded enzyme, feruloyl esterase B (FAEB), does not have tannase activity. Comparison of the physical characteristics and substrate specificity of FAEB with those of a cinnamoyl esterase from A. niger [Kroon, Faulds and Williamson (1996) Biotechnol. Appl. Biochem. 23, 255-262] suggests that they are in fact the same enzyme. The expression of faeB is specifically induced in the presence of certain aromatic compounds, but not in the presence of other constituents present in plant-cell-wall polysaccharides such as arabinoxylan or pectin. The expression profile of faeB in the presence of aromatic compounds was compared with the expression of A. niger faeA, encoding feruloyl esterase A (FAEA), and A. niger bphA, the gene encoding a benzoate-p-hydroxylase. All three genes have different subsets of aromatic compounds that induce their expression, indicating the presence of different transcription activating systems in A. niger that respond to aromatic compounds. Comparison of the activity of FAEA and FAEB on sugar-beet pectin and wheat arabinoxylan demonstrated that they are both involved in the degradation of both polysaccharides, but have opposite preferences for these substrates. FAEA is more active than FAEB towards wheat arabinoxylan, whereas FAEB is more active than FAEA towards sugar-beet pectin.
ESTHER : de Vries_2002_Biochem.J_363_377
PubMedSearch : de Vries_2002_Biochem.J_363_377
PubMedID: 11931668
Gene_locus related to this paper: aspng-faeb

Title : Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation - Ademark_2001_Eur.J.Biochem_268_2982
Author(s) : Ademark P , de Vries RP , Hagglund P , Stalbrand H , Visser J
Ref : European Journal of Biochemistry , 268 :2982 , 2001
Abstract : Alpha-galactosidase (EC and beta-mannosidase (EC participate in the hydrolysis of complex plant saccharides such as galacto(gluco)mannans. Here we report on the cloning and characterization of genes encoding an alpha-galactosidase (AglC) and a beta-mannosidase (MndA) from Aspergillus niger. The aglC and mndA genes code for 747 and 931 amino acids, respectively, including the eukaryotic signal sequences. The predicted isoelectric points of AglC and MndA are 4.56 and 5.17, and the calculated molecular masses are 79.674 and 102.335 kDa, respectively. Both AglC and MndA contain several putative N-glycosylation sites. AglC was assigned to family 36 of the glycosyl hydrolases and MndA was assigned to family 2. The expression patterns of aglC and mndA and two other genes encoding A. niger alpha-galactosidases (aglA and aglB) during cultivation on galactomannan were studied by Northern analysis. A comparison of gene expression on monosaccharides in the A. niger wild-type and a CreA mutant strain showed that the carbon catabolite repressor protein CreA has a strong influence on aglA, but not on aglB, aglC or mndA. AglC and MndA were purified from constructed overexpression strains of A. niger, and the combined action of these enzymes degraded a galactomanno-oligosaccharide into galactose and mannose. The possible roles of AglC and MndA in galactomannan hydrolysis is discussed.
ESTHER : Ademark_2001_Eur.J.Biochem_268_2982
PubMedSearch : Ademark_2001_Eur.J.Biochem_268_2982
PubMedID: 11358516

Title : Aspergillus enzymes involved in degradation of plant cell wall polysaccharides - de Vries_2001_Microbiol.Mol.Biol.Rev_65_497
Author(s) : de Vries RP , Visser J
Ref : Microbiol Mol Biol Rev , 65 :497 , 2001
Abstract : Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.
ESTHER : de Vries_2001_Microbiol.Mol.Biol.Rev_65_497
PubMedSearch : de Vries_2001_Microbiol.Mol.Biol.Rev_65_497
PubMedID: 11729262

Title : The Aspergillus niger D-xylulose kinase gene is co-expressed with genes encoding arabinan degrading enzymes, and is essential for growth on D-xylose and L-arabinose - vanKuyk_2001_Eur.J.Biochem_268_5414
Author(s) : vanKuyk PA , de Groot MJ , Ruijter GJ , de Vries RP , Visser J
Ref : European Journal of Biochemistry , 268 :5414 , 2001
Abstract : The Aspergillus niger D-xylulose kinase encoding gene has been cloned by complementation of a strain deficient in D-xylulose kinase activity. Expression of xkiA was observed in the presence of L-arabinose, L-arabitol and D-xylose. Expression of xkiA is not mediated by XLNR, the xylose-dependent positively-acting xylanolytic regulator. Although the expression of xkiA is subject to carbon catabolite repression, the wide domain regulator CREA is not directly involved. The A. niger D-xylulose kinase was purified to homogeneity, and the molecular mass determined using electrospray ionization mass spectrometry agreed with the calculated molecular mass of 62816.6 Da. The activity of XKIA is highly specific for D-xylulose. Kinetic parameters were determined as Km(D-xylulose) = 0.76 mM and Km(ATP) = 0.061 mM. Increased transcript levels of the genes encoding arabinan and xylan degrading enzymes, observed in the xylulose kinase deficient strain, correlate with increased accumulation of L-arabitol and xylitol, respectively. This result supports the suggestion that L-arabitol may be the specific low molecular mass inducer of the genes involved in arabinan degradation. It also suggests a possible role for xylitol in the induction of xylanolytic genes. Conversely, overproduction of XKIA did not reduce the size of the intracellular arabitol and xylitol pools, and therefore had no effect on expression of genes encoding xylan and arabinan degrading enzymes nor on the activity of the enzymes of the catabolic pathway.
ESTHER : vanKuyk_2001_Eur.J.Biochem_268_5414
PubMedSearch : vanKuyk_2001_Eur.J.Biochem_268_5414
PubMedID: 11606204

Title : Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides - de Vries_2000_Carbohydr.Res_327_401
Author(s) : de Vries RP , Kester HC , Poulsen CH , Benen JA , Visser J
Ref : Carbohydr Res , 327 :401 , 2000
Abstract : Synergy in the degradation of two plant cell wall polysaccharides, water insoluble pentosan from wheat flour (an arabinoxylan) and sugar beet pectin, was studied using several main-chain cleaving and accessory enzymes. Synergy was observed between most enzymes tested, although not always to the same extent. Degradation of the xylan backbone by endo-xylanase and beta-xylosidase was influenced most strongly by the action of alpha-L-arabinofuranosidase and arabinoxylan arabinofuranohydrolase resulting in a 2.5-fold and twofold increase in release of xylose, respectively. Ferulic acid release by feruloyl esterase A and 4-O-methyl glucuronic acid release by alpha-glucuronidase depended largely on the degradation of the xylan backbone by endo-xylanase but were also influenced by other enzymes. Degradation of the backbone of the pectin hairy regions resulted in a twofold increase in the release of galactose by beta-galactosidase and endo-galactanase but did not significantly influence the arabinose release by arabinofuranosidase and endo-arabinase. Ferulic acid release from sugar beet pectin by feruloyl esterase A was affected most strongly by the presence of other accessory enzymes.
ESTHER : de Vries_2000_Carbohydr.Res_327_401
PubMedSearch : de Vries_2000_Carbohydr.Res_327_401
PubMedID: 10990025

Title : Inverting character of alpha-glucuronidase A from Aspergillus tubingensis - Biely_2000_Biochim.Biophys.Acta_1474_360
Author(s) : Biely P , de Vries RP , Vrsanska M , Visser J
Ref : Biochimica & Biophysica Acta , 1474 :360 , 2000
Abstract : Alpha-glucuronidase A from Aspergillus tubingensis was found to be capable of liberating 4-O-methyl-D-glucuronic acid (MeGlcA) only from those beechwood glucuronoxylan fragments in which the acid is attached to the non-reducing terminal xylopyranosyl residue. Reduced aldotetrauronic acid, 4-O-methyl-D-glucuronosyl-alpha-1,2-D-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1 ,4-xylitol, was found to be a suitable substrate to follow the stereochemical course of the hydrolytic reaction catalyzed by the purified enzyme. The configuration of the liberated MeGlcA was followed in a D(2)O reaction mixture by (1)H-NMR spectroscopy. It was unambiguously established that MeGlcA was released from the substrate as its beta-anomer from which the alpha-anomer was formed on mutarotation. This result represents the first experimental evidence for the inverting character of a microbial alpha-glucuronidase, a member of glycosyl hydrolase family 67 (EC
ESTHER : Biely_2000_Biochim.Biophys.Acta_1474_360
PubMedSearch : Biely_2000_Biochim.Biophys.Acta_1474_360
PubMedID: 10779688

Title : Differential expression of three alpha-galactosidase genes and a single beta-galactosidase gene from Aspergillus niger - de Vries_1999_Appl.Environ.Microbiol_65_2453
Author(s) : de Vries RP , van den Broeck HC , Dekkers E , Manzanares P , De Graaff LH , Visser J
Ref : Applied Environmental Microbiology , 65 :2453 , 1999
Abstract : A gene encoding a third alpha-galactosidase (AglB) from Aspergillus niger has been cloned and sequenced. The gene consists of an open reading frame of 1,750 bp containing six introns. The gene encodes a protein of 443 amino acids which contains a eukaryotic signal sequence of 16 amino acids and seven putative N-glycosylation sites. The mature protein has a calculated molecular mass of 48,835 Da and a predicted pI of 4.6. An alignment of the AglB amino acid sequence with those of other alpha-galactosidases revealed that it belongs to a subfamily of alpha-galactosidases that also includes A. niger AglA. A. niger AglC belongs to a different subfamily that consists mainly of prokaryotic alpha-galactosidases. The expression of aglA, aglB, aglC, and lacA, the latter of which encodes an A. niger beta-galactosidase, has been studied by using a number of monomeric, oligomeric, and polymeric compounds as growth substrates. Expression of aglA is only detected on galactose and galactose-containing oligomers and polymers. The aglB gene is expressed on all of the carbon sources tested, including glucose. Elevated expression was observed on xylan, which could be assigned to regulation via XlnR, the xylanolytic transcriptional activator. Expression of aglC was only observed on glucose, fructose, and combinations of glucose with xylose and galactose. High expression of lacA was detected on arabinose, xylose, xylan, and pectin. Similar to aglB, the expression on xylose and xylan can be assigned to regulation via XlnR. All four genes have distinct expression patterns which seem to mirror the natural substrates of the encoded proteins.
ESTHER : de Vries_1999_Appl.Environ.Microbiol_65_2453
PubMedSearch : de Vries_1999_Appl.Environ.Microbiol_65_2453
PubMedID: 10347026

Title : Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger - de Vries_1999_Appl.Environ.Microbiol_65_5500
Author(s) : de Vries RP , Visser J
Ref : Applied Environmental Microbiology , 65 :5500 , 1999
Abstract : Feruloyl esterases can remove aromatic residues (e.g., ferulic acid) from plant cell wall polysaccharides (xylan, pectin) and are essential for complete degradation of these polysaccharides. Expression of the feruloyl esterase-encoding gene (faeA) from Aspergillus niger depends on D-xylose (expression is mediated by XlnR, the xylanolytic transcriptional activator) and on a second system that responds to aromatic compounds with a defined ring structure, such as ferulic acid and vanillic acid. Several compounds were tested, and all of the inducing compounds contained a benzene ring which had a methoxy group at C-3 and a hydroxy group at C-4 but was not substituted at C-5. Various aliphatic groups occurred at C-1. faeA expression in the presence of xylose or ferulic acid was repressed by glucose. faeA expression in the presence of ferulic acid and xylose was greater than faeA expression in the presence of either compound alone. The various inducing systems allow A. niger to produce feruloyl esterase not only during growth on xylan but also during growth on other ferulic acid-containing cell wall polysaccharides, such as pectin.
ESTHER : de Vries_1999_Appl.Environ.Microbiol_65_5500
PubMedSearch : de Vries_1999_Appl.Environ.Microbiol_65_5500
PubMedID: 10584009

Title : CreA modulates the XlnR-induced expression on xylose of Aspergillus niger genes involved in xylan degradation - de Vries_1999_Res.Microbiol_150_281
Author(s) : de Vries RP , Visser J , De Graaff LH
Ref : Res Microbiol , 150 :281 , 1999
Abstract : The expression of the feruloyl esterase gene faeA, the alpha-glucuronidase gene aguA, the endoxylanase gene xlnB, and the beta-xylosidase gene xlnD from Aspergillus niger on xylose was studied in a wild-type strain and in a CreA mutant. A decrease in expression of all four genes was observed with increasing xylose concentrations in the wild-type strain, whereas expression levels in the CreA mutant were not influenced. The results in the wild type indicated that xylose concentrations higher than 1 mM resulted in repression of the expression of the xylanolytic genes tested mediated by the carbon catabolite repressor protein CreA. On xylose, the expression levels of the xylanolytic genes were therefore not only determined by induction via XlnR, but also by repression via CreA. The genes tested were not influenced to the same extent by XlnR or CreA, resulting in specific expression levels and patterns for each individual gene.
ESTHER : de Vries_1999_Res.Microbiol_150_281
PubMedSearch : de Vries_1999_Res.Microbiol_150_281
PubMedID: 10376490

Title : Stability of feruloyl esterases from Aspergillus -
Author(s) : Faulds CB , de Vries RP , Visser J , Williamson G
Ref : Biochemical Society Transactions , 26 :S165 , 1998
PubMedID: 9649840

Title : aguA, the gene encoding an extracellular alpha-glucuronidase from Aspergillus tubingensis, is specifically induced on xylose and not on glucuronic acid - de Vries_1998_J.Bacteriol_180_243
Author(s) : de Vries RP , Poulsen CH , Madrid S , Visser J
Ref : Journal of Bacteriology , 180 :243 , 1998
Abstract : An extracellular alpha-glucuronidase was purified and characterized from a commercial Aspergillus preparation and from culture filtrate of Aspergillus tubingensis. The enzyme has a molecular mass of 107 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 112 kDa as determined by mass spectrometry, has a determined pI just below 5.2, and is stable at pH 6.0 for prolonged times. The pH optimum for the enzyme is between 4.5 and 6.0, and the temperature optimum is 70 degrees C. The alpha-glucuronidase is active mainly on small substituted xylo-oligomers but is also able to release a small amount of 4-O-methylglucuronic acid from birchwood xylan. The enzyme acts synergistically with endoxylanases and beta-xylosidase in the hydrolysis of xylan. The enzyme is N glycosylated and contains 14 putative N-glycosylation sites. The gene encoding this alpha-glucuronidase (aguA) was cloned from A. tubingensis. It consists of an open reading frame of 2,523 bp and contains no introns. The gene codes for a protein of 841 amino acids, containing a eukaryotic signal sequence of 20 amino acids. The mature protein has a predicted molecular mass of 91,790 Da and a calculated pI of 5.13. Multiple copies of the gene were introduced in A. tubingensis, and expression was studied in a highly overproducing transformant. The aguA gene was expressed on xylose, xylobiose, and xylan, similarly to genes encoding endoxylanases, suggesting a coordinate regulation of expression of xylanases and alpha-glucuronidase. Glucuronic acid did not induce the expression of aguA and also did not modulate the expression on xylose. Addition of glucose prevented expression of aguA on xylan but only reduced the expression on xylose.
ESTHER : de Vries_1998_J.Bacteriol_180_243
PubMedSearch : de Vries_1998_J.Bacteriol_180_243
PubMedID: 9440512

Title : The transcriptional activator XlnR regulates both xylanolytic and endoglucanase gene expression in Aspergillus niger - van Peij_1998_Appl.Environ.Microbiol_64_3615
Author(s) : van Peij NN , Gielkens MM , de Vries RP , Visser J , De Graaff LH
Ref : Applied Environmental Microbiology , 64 :3615 , 1998
Abstract : The expression of genes encoding enzymes involved in xylan degradation and two endoglucanases involved in cellulose degradation was studied at the mRNA level in the filamentous fungus Aspergillus niger. A strain with a loss-of-function mutation in the xlnR gene encoding the transcriptional activator XlnR and a strain with multiple copies of this gene were investigated in order to define which genes are controlled by XlnR. The data presented in this paper show that the transcriptional activator XlnR regulates the transcription of the xlnB, xlnC, and xlnD genes encoding the main xylanolytic enzymes (endoxylanases B and C and beta-xylosidase, respectively). Also, the transcription of the genes encoding the accessory enzymes involved in xylan degradation, including alpha-glucuronidase A, acetylxylan esterase A, arabinoxylan arabinofuranohydrolase A, and feruloyl esterase A, was found to be controlled by XlnR. In addition, XlnR also activates transcription of two endoglucanase-encoding genes, eglA and eglB, indicating that transcriptional regulation by XlnR goes beyond the genes encoding xylanolytic enzymes and includes regulation of two endoglucanase-encoding genes.
ESTHER : van Peij_1998_Appl.Environ.Microbiol_64_3615
PubMedSearch : van Peij_1998_Appl.Environ.Microbiol_64_3615
PubMedID: 9758775

Title : Influence of ferulic acid on the production of feruloyl esterases by Aspergillus niger - Faulds_1997_FEMS.Microbiol.Lett_157_239
Author(s) : Faulds CB , de Vries RP , Kroon PA , Visser J , Williamson G
Ref : FEMS Microbiology Letters , 157 :239 , 1997
Abstract : Extracellular feruloyl esterases from the filamentous fungus Aspergillus niger are induced by growth on oat spelt xylan (OSX), which contains no detectable esterified ferulic acid. FAE-III accounted for most of the feruloyl esterase activity. Addition of free ferulic acid to OSX at the start of the culture induced FAE-III secretion a further 2.3-fold, and also induced other feruloyl esterases which could not be ascribed to FAE-III. Wheat bran-(WB)-grown cultures, containing 1% (m/v) esterlinked ferulic acid, gave almost identical FAE-III and total feruloyl esterase activities as the cultures grown on OSX plus ferulic acid. De-esterification of WB yielded less total feruloyl esterase, and 2.4-fold less FAE-III, compared to untreated WB. A slightly modified form of FAE-III was produced on de-esterified WB. These results show that production of FAE-III does not absolutely require ferulic acid. However, production is stimulated by the presence of free ferulic acid through increased expression, and is reduced by the removal of esterified ferulic acid from the growth substrate.
ESTHER : Faulds_1997_FEMS.Microbiol.Lett_157_239
PubMedSearch : Faulds_1997_FEMS.Microbiol.Lett_157_239
PubMedID: 9435103

Title : The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides - de Vries_1997_Appl.Environ.Microbiol_63_4638
Author(s) : de Vries RP , Michelsen B , Poulsen CH , Kroon PA , van den Heuvel RH , Faulds CB , Williamson G , van den Hombergh JP , Visser J
Ref : Applied Environmental Microbiology , 63 :4638 , 1997
Abstract : We report the cloning and characterization of a gene encoding a ferulic acid esterase, faeA, from Aspergillus niger and Aspergillus tubingensis. The A. niger and A. tubingensis genes have a high degree of sequence identity and contain one conserved intron. The gene product, FAEA, was overexpressed in wild-type A. tubingensis and a protease-deficient A. niger mutant. Overexpression of both genes in wild-type A. tubingensis and an A. niger protease-deficient mutant showed that the A. tubingensis gene product is more sensitive to degradation than the equivalent gene product from A. niger. FAEA from A. niger was identical to A. niger FAE-III (C. B. Faulds and G. Williamson, Microbiology 140:779-787, 1994), as assessed by molecular mass, pH and temperature optima, pI, N-terminal sequence, and activity on methyl ferulate. The faeA gene was induced by growth on wheat arabinoxylan and sugar beet pectin, and its gene product (FAEA) released ferulic acid from wheat arabinoxylan. The rate of release was enhanced by the presence of a xylanase. FAEA also hydrolyzed smaller amounts of ferulic acid from sugar beet pectin, but the rate was hardly affected by addition of an endo-pectin lyase.
ESTHER : de Vries_1997_Appl.Environ.Microbiol_63_4638
PubMedSearch : de Vries_1997_Appl.Environ.Microbiol_63_4638
PubMedID: 9406381
Gene_locus related to this paper: aspni-FAEA , asptu-FAEA

Title : Characterization of an Aspergillus nidulans L-arabitol dehydrogenase mutant - de Vries_1994_FEMS.Microbiol.Lett_123_83
Author(s) : de Vries RP , Flipphi MJ , Witteveen CF , Visser J
Ref : FEMS Microbiology Letters , 123 :83 , 1994
Abstract : The degradation pathway for L-arabinose, which consists of a sequence of alternating reduction and oxidation reactions prior to ultimate phosphorylation, was studied in Aspergillus nidulans wild-type as well as in an L-arabinose non-utilizing mutant. The inability of the mutant to use L-arabinose was caused by the absence of L-arabitol dehydrogenase activity. The effect of the mutation on polyol accumulation patterns was studied upon growth on various carbon sources. The presence of L-arabinose resulted in intracellular accumulation of arabitol in this mutant. Moreover, the mutant secreted arabitol under these conditions and, in contrast to the wild-type, featured enhanced expression of enzymes involved in L-arabinose catabolism as well as of extracellular glycosyl hydrolases involved in degradation of the plant cell wall polysaccharide L-arabinan.
ESTHER : de Vries_1994_FEMS.Microbiol.Lett_123_83
PubMedSearch : de Vries_1994_FEMS.Microbiol.Lett_123_83
PubMedID: 7988903

Title : In vitro immune responsiveness to vaccinea virus and HLA - de Vries_1977_N.Engl.J.Med_297_692
Author(s) : de Vries RP , Kreeftenberg HG , Loggen HG , van Rood JJ
Ref : N Engl J Med , 297 :692 , 1977
Abstract : Because several lines of evidence suggest that HLA products might have an important function in the immune response to infectious agents, we studied the possible relation between immune response to vaccinia virus and HLA phenotype in 79 soldiers who received a primary vaccination. A low in vitro response to vaccinia virus was associated with HLA-Cw3 both in 49 subjects tested three to four weeks after vaccination (P less than 0.001) and in the remaining 30 subjects tested five to 11 weeks after vaccination (P = 0.035). Responses to unrelated antigens and phytohemagglutinin of lymphocytes tested before, three to four weeks and five to 11 weeks after vaccination indicated that this association was specific for vaccinia virus and suggested that differences in immune response to vaccinia were reflected in temporarily altered immune responsiveness to unrelated antigens. Our results indicate that HLA-Cw3 or an HLA product associated with Cw3 is involved in the cellular immune response to vaccinia virus.
ESTHER : de Vries_1977_N.Engl.J.Med_297_692
PubMedSearch : de Vries_1977_N.Engl.J.Med_297_692
PubMedID: 70749