Punt PJ

References (6)

Title : Utilization of ferulic acid in Aspergillus niger requires the transcription factor FarA and a newly identified Far-like protein (FarD) that lacks the canonical Zn(II)(2)Cys(6) domain - Arentshorst_2022_Front.Fungal.Biol_3_978845
Author(s) : Arentshorst M , Reijngoud J , van Tol DJC , Reid ID , Arendsen Y , Pel HJ , van Peij N , Visser J , Punt PJ , Tsang A , Ram AFJ
Ref : Front Fungal Biol , 3 :978845 , 2022
Abstract : The feruloyl esterase B gene (faeB) is specifically induced by hydroxycinnamic acids (e.g. ferulic acid, caffeic acid and coumaric acid) but the transcriptional regulation network involved in faeB induction and ferulic acid metabolism has only been partially addressed. To identify transcription factors involved in ferulic acid metabolism we constructed and screened a transcription factor knockout library of 239 Aspergillus niger strains for mutants unable to utilize ferulic acid as a carbon source. The deltafarA transcription factor mutant, already known to be involved in fatty acid metabolism, could not utilize ferulic acid and other hydroxycinnamic acids. In addition to screening the transcription factor mutant collection, a forward genetic screen was performed to isolate mutants unable to express faeB. For this screen a PfaeB-amdS and PfaeB-lux(613) dual reporter strain was engineered. The rationale of the screen is that in this reporter strain ferulic acid induces amdS (acetamidase) expression via the faeB promoter resulting in lethality on fluoro-acetamide. Conidia of this reporter strain were UV-mutagenized and plated on fluoro-acetamide medium in the presence of ferulic acid. Mutants unable to induce faeB are expected to be fluoro-acetamide resistant and can be positively selected for. Using this screen, six fluoro-acetamide resistant mutants were obtained and phenotypically characterized. Three mutants had a phenotype identical to the farA mutant and sequencing the farA gene in these mutants indeed showed mutations in FarA which resulted in inability to growth on ferulic acid as well as on short and long chain fatty acids. The growth phenotype of the other three mutants was similar to the farA mutants in terms of the inability to grow on ferulic acid, but these mutants grew normally on short and long chain fatty acids. The genomes of these three mutants were sequenced and allelic mutations in one particular gene (NRRL3_09145) were found. The protein encoded by NRRL3_09145 shows similarity to the FarA and FarB transcription factors. However, whereas FarA and FarB contain both the Zn(II)(2)Cys(6) domain and a fungal-specific transcription factor domain, the protein encoded by NRRL3_09145 (FarD) lacks the canonical Zn(II)(2)Cys(6) domain and possesses only the fungal specific transcription factor domain.
ESTHER : Arentshorst_2022_Front.Fungal.Biol_3_978845
PubMedSearch : Arentshorst_2022_Front.Fungal.Biol_3_978845
PubMedID: 37746181
Gene_locus related to this paper: aspng-faeb

Title : Loss of function of the carbon catabolite repressor CreA leads to low but inducer-independent expression from the feruloyl esterase B promoter in Aspergillus niger - Reijngoud_2021_Biotechnol.Lett__
Author(s) : Reijngoud J , Arentshorst M , Ruijmbeek C , Reid I , Alazi ED , Punt PJ , Tsang A , Ram AFJ
Ref : Biotechnol Lett , : , 2021
Abstract : OBJECTIVE: With the aim to decipher the mechanisms involved in the transcriptional regulation of feruloyl esterase encoded by faeB, a genetic screen was performed to isolate A. niger mutants displaying inducer-independent expression from the faeB promoter. RESULT: PfaeB-amdS and PfaeB-lux dual reporter strains were constructed and used to isolate trans-acting mutants in which the expression of both reporters was increased, based on the ability to grow on acetamide plates and higher luciferase activity, respectively. The genetic screen on the non-inducing carbon source D-fructose yielded in total 111 trans-acting mutants. The genome of one of the mutants was sequenced and revealed several SNPs, including a point mutation in the creA gene encoding a transcription factor known to be involved in carbon catabolite repression. Subsequently, all mutants were analyzed for defects in carbon catabolite repression by determining sensitivity towards allyl alcohol. All except four of the 111 mutants were sensitive to allyl alcohol, indicating that the vast majority of the mutants are defective in carbon catabolite repression. The creA gene of 32 allyl alcohol sensitive mutants was sequenced and 27 of them indeed contained a mutation in the creA gene. Targeted deletion of creA in the reporter strain confirmed that the loss of CreA results in constitutive expression from the faeB promoter. CONCLUSION: Loss of function of CreA leads to low but inducer-independent expression from the faeB promoter in A. niger.
ESTHER : Reijngoud_2021_Biotechnol.Lett__
PubMedSearch : Reijngoud_2021_Biotechnol.Lett__
PubMedID: 33738610

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 : Development of a mature fungal technology and production platform for industrial enzymes based on a Myceliophthora thermophila isolate, previously known as Chrysosporium lucknowense C1 - Visser_2011_Industrial.Biotechnology_7_214
Author(s) : Visser H , Joosten V , Punt PJ , Gusakov AV , Olson PT , Joosten R
Ref : Industrial Biotechnology , 7 :214 , 2011
Abstract : The filamentous fungus C1 was developed into an expression platform for screening and production of diverse industrial enzymes. C1 shows a low-viscosity morphology in submerged culture, enabling the use of complex growth and production media. This morphology furthermore allowed C1 to be used as a host for high-throughput robotic screening of gene libraries. A C1-genetic toolbox was developed, which enabled the generation of a large collection of dedicated C1 host strains and gene-expression strategies. The 38 Mbp genome was sequenced and found to be rich in biomass-hydrolyzingenzyme- encoding genes. C1 production strains have been developed that produce large quantities of these enzyme mixtures (up to 100 g/L total protein). Recombinant C1 strains were constructed that produce single enzymes in a relatively pure form, facilitating enzyme purification and characterization, as well as for commercial applications. Molecular phylogenetic studies revealed that C1, previously classified as Chrysosporium lucknowense based on morphological characteristics, is actually a Myceliophthora thermophila isolate. In addition, C1 has proven to be a source of novel industrial enzymes, and the C1-technology platform developed has been applied as a tool for research on and production of industrial enzymes for various industrial applications, such as biofuels and biorefineries.
ESTHER : Visser_2011_Industrial.Biotechnology_7_214
PubMedSearch : Visser_2011_Industrial.Biotechnology_7_214
PubMedID:

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 : Regulation of expression of the Aspergillus niger benzoate para-hydroxylase cytochrome P450 system - van den Brink_2000_Mol.Gen.Genet_263_601
Author(s) : van den Brink JM , Punt PJ , van Gorcom RF , van den Hondel CA
Ref : Molecular & General Genetics , 263 :601 , 2000
Abstract : Cytochrome P450 enzyme systems are found throughout nature and are involved in many different, often complex, bioconversions. In the endoplasmic reticulum of the filamentous fungus Aspergillus niger a cytochrome P450 enzyme system is present that is capable of the para-hydroxylation of benzoate. The expression of the two genes encoding the components of this system, the cytochrome P450 gene encoding benzoate para-hydroxylase (bphA) and the gene encoding cytochrome P450 reductase (cprA), is inducible by benzoate. The BPH system was used as a model system to study the mechanisms that result in co-regulation of both components of an eukaryote cytochrome P450 enzyme system. Deletion analysis of the transcription control regions of cprA and bphA resulted in the identification of a region that was involved in benzoate induction of gene expression. The functional competence of the cprA Benzoate Responsive Region thus defined was demonstrated directly by cloning this fragment upstream of a constitutively expressed mini-promoter and analysing expression of the hybrid transcription control region in a lacZ reporter system. Further analysis of cprA gene expression revealed a clear quantitative discrepancy between induction at the protein level (approximately 4-fold) and at the transcription level (> 20-fold). The majority of the transcripts observed after benzoate induction (cprAbeta) were larger then the constitutively expressed cprAalpha transcript. The difference in size between the cprAalpha and cprAbeta transcript is caused by differential promoter use. As the longer cprAbeta transcript carries a small uORF we propose that post-transcriptional regulation of CPR expression underlies the discrepancy in the degree of induction at the protein and transcriptional level. Our results show that regulation of CPR expression is particularly complex, involving regulatory promoter elements, differential promoter use and regulation at the post-transcriptional level.
ESTHER : van den Brink_2000_Mol.Gen.Genet_263_601
PubMedSearch : van den Brink_2000_Mol.Gen.Genet_263_601
PubMedID: 10852481