Master E

References (4)

Title : Elucidating Sequence and Structural Determinants of Carbohydrate Esterases for Complete Deacetylation of Substituted Xylans - Penttinen_2022_Molecules_27_
Author(s) : Penttinen L , Kouhi V , Faure R , Skarina T , Stogios P , Master E , Jurak E
Ref : Molecules , 27 : , 2022
Abstract : Acetylated glucuronoxylan is one of the most common types of hemicellulose in nature. The structure is formed by a beta-(14)-linked D-xylopyranosyl (Xylp) backbone that can be substituted with an acetyl group at O-2 and O-3 positions, and alpha-(1->2)-linked 4-O-methylglucopyranosyluronic acid (MeGlcpA). Acetyl xylan esterases (AcXE) that target mono- or doubly acetylated Xylp are well characterized; however, the previously studied AcXE from Flavobacterium johnsoniae (FjoAcXE) was the first to remove the acetyl group from 2-O-MeGlcpA-3-O-acetyl-substituted Xylp units, yet structural characteristics of these enzymes remain unspecified. Here, six homologs of FjoAcXE were produced and three crystal structures of the enzymes were solved. Two of them are complex structures, one with bound MeGlcpA and another with acetate. All homologs were confirmed to release acetate from 2-O-MeGlcpA-3-O-acetyl-substituted xylan, and the crystal structures point to key structural elements that might serve as defining features of this unclassified carbohydrate esterase family. Enzymes comprised two domains: N-terminal CBM domain and a C-terminal SGNH domain. In FjoAcXE and all studied homologs, the sequence motif around the catalytic serine is Gly-Asn-Ser-Ile (GNSI), which differs from other SGNH hydrolases. Binding by the MeGlcpA-Xylp ligand is directed by positively charged and highly conserved residues at the interface of the CBM and SGNH domains of the enzyme.
ESTHER : Penttinen_2022_Molecules_27_
PubMedSearch : Penttinen_2022_Molecules_27_
PubMedID: 35566004

Title : Analysis of the Phlebiopsis gigantea genome, transcriptome and secretome provides insight into its pioneer colonization strategies of wood - Hori_2014_PLoS.Genet_10_e1004759
Author(s) : Hori C , Ishida T , Igarashi K , Samejima M , Suzuki H , Master E , Ferreira P , Ruiz-Duenas FJ , Held B , Canessa P , Larrondo LF , Schmoll M , Druzhinina IS , Kubicek CP , Gaskell JA , Kersten P , St John F , Glasner J , Sabat G , Splinter BonDurant S , Syed K , Yadav J , Mgbeahuruike AC , Kovalchuk A , Asiegbu FO , Lackner G , Hoffmeister D , Rencoret J , Gutierrez A , Sun H , Lindquist E , Barry K , Riley R , Grigoriev IV , Henrissat B , Kues U , Berka RM , Martinez AT , Covert SF , Blanchette RA , Cullen D
Ref : PLoS Genet , 10 :e1004759 , 2014
Abstract : Collectively classified as white-rot fungi, certain basidiomycetes efficiently degrade the major structural polymers of wood cell walls. A small subset of these Agaricomycetes, exemplified by Phlebiopsis gigantea, is capable of colonizing freshly exposed conifer sapwood despite its high content of extractives, which retards the establishment of other fungal species. The mechanism(s) by which P. gigantea tolerates and metabolizes resinous compounds have not been explored. Here, we report the annotated P. gigantea genome and compare profiles of its transcriptome and secretome when cultured on fresh-cut versus solvent-extracted loblolly pine wood. The P. gigantea genome contains a conventional repertoire of hydrolase genes involved in cellulose/hemicellulose degradation, whose patterns of expression were relatively unperturbed by the absence of extractives. The expression of genes typically ascribed to lignin degradation was also largely unaffected. In contrast, genes likely involved in the transformation and detoxification of wood extractives were highly induced in its presence. Their products included an ABC transporter, lipases, cytochrome P450s, glutathione S-transferase and aldehyde dehydrogenase. Other regulated genes of unknown function and several constitutively expressed genes are also likely involved in P. gigantea's extractives metabolism. These results contribute to our fundamental understanding of pioneer colonization of conifer wood and provide insight into the diverse chemistries employed by fungi in carbon cycling processes.
ESTHER : Hori_2014_PLoS.Genet_10_e1004759
PubMedSearch : Hori_2014_PLoS.Genet_10_e1004759
PubMedID: 25474575
Gene_locus related to this paper: phlgi-a0a0c3nds0 , phlgi-a0a0c3niq6 , phlgi-a0a0c3pc91 , phlgi-a0a0c3pv58 , phlgi-a0a0c3rra0 , phlgi-a0a0c3rvc4 , phlgi-a0a0c3rvu0 , phlgi-a0a0c3s394 , phlgi-a0a0c3s606 , phlgi-a0a0c3s673 , phlgi-a0a0c3s8d3 , phlgi-a0a0c3sce4 , phlgi-a0a0c3sdt8

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 : Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion - Martinez_2009_Proc.Natl.Acad.Sci.U.S.A_106_1954
Author(s) : Martinez D , Challacombe J , Morgenstern I , Hibbett D , Schmoll M , Kubicek CP , Ferreira P , Ruiz-Duenas FJ , Martinez AT , Kersten P , Hammel KE , Vanden Wymelenberg A , Gaskell J , Lindquist E , Sabat G , Bondurant SS , Larrondo LF , Canessa P , Vicuna R , Yadav J , Doddapaneni H , Subramanian V , Pisabarro AG , Lavin JL , Oguiza JA , Master E , Henrissat B , Coutinho PM , Harris P , Magnuson JK , Baker SE , Bruno K , Kenealy W , Hoegger PJ , Kues U , Ramaiya P , Lucas S , Salamov A , Shapiro H , Tu H , Chee CL , Misra M , Xie G , Teter S , Yaver D , James T , Mokrejs M , Pospisek M , Grigoriev IV , Brettin T , Rokhsar D , Berka R , Cullen D
Ref : Proc Natl Acad Sci U S A , 106 :1954 , 2009
Abstract : Brown-rot fungi such as Postia placenta are common inhabitants of forest ecosystems and are also largely responsible for the destructive decay of wooden structures. Rapid depolymerization of cellulose is a distinguishing feature of brown-rot, but the biochemical mechanisms and underlying genetics are poorly understood. Systematic examination of the P. placenta genome, transcriptome, and secretome revealed unique extracellular enzyme systems, including an unusual repertoire of extracellular glycoside hydrolases. Genes encoding exocellobiohydrolases and cellulose-binding domains, typical of cellulolytic microbes, are absent in this efficient cellulose-degrading fungus. When P. placenta was grown in medium containing cellulose as sole carbon source, transcripts corresponding to many hemicellulases and to a single putative beta-1-4 endoglucanase were expressed at high levels relative to glucose-grown cultures. These transcript profiles were confirmed by direct identification of peptides by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Also up-regulated during growth on cellulose medium were putative iron reductases, quinone reductase, and structurally divergent oxidases potentially involved in extracellular generation of Fe(II) and H(2)O(2). These observations are consistent with a biodegradative role for Fenton chemistry in which Fe(II) and H(2)O(2) react to form hydroxyl radicals, highly reactive oxidants capable of depolymerizing cellulose. The P. placenta genome resources provide unparalleled opportunities for investigating such unusual mechanisms of cellulose conversion. More broadly, the genome offers insight into the diversification of lignocellulose degrading mechanisms in fungi. Comparisons with the closely related white-rot fungus Phanerochaete chrysosporium support an evolutionary shift from white-rot to brown-rot during which the capacity for efficient depolymerization of lignin was lost.
ESTHER : Martinez_2009_Proc.Natl.Acad.Sci.U.S.A_106_1954
PubMedSearch : Martinez_2009_Proc.Natl.Acad.Sci.U.S.A_106_1954
PubMedID: 19193860
Gene_locus related to this paper: pospm-b8p1f3 , pospm-b8p2q7 , pospm-b8p4n0 , pospm-b8p4n9 , pospm-b8p5g9 , pospm-b8p5r9 , pospm-b8p6h2 , pospm-b8p7b1 , pospm-b8p7c4 , pospm-b8p8w7 , pospm-b8p9j1 , pospm-b8p164 , pospm-b8p280 , pospm-b8p423.1 , pospm-b8p423.2 , pospm-b8p858 , pospm-b8pam2 , pospm-b8pam5 , pospm-b8pb68 , pospm-b8pbm3 , pospm-b8pc54 , pospm-b8pc56 , pospm-b8pce4 , pospm-b8pd91 , pospm-b8pdk6 , pospm-b8ph32 , pospm-b8ph43 , pospm-b8phc9 , pospm-b8php7 , pospm-b8phy5 , pospm-b8pjg8 , pospm-b8pji9 , pospm-b8plr5 , pospm-b8pmk3 , pospm-b8pfg0 , pospm-b8pg35 , pospm-b8pa20.1 , pospm-b8pa20.2 , pospm-b8p4g8 , pospm-b8phn6