Skip to Main Content
Computational analysis of the Phanerochaete chrysosporium v2.0 genome database and mass spectrometry identiWcation of peptides in ligninolytic cultures reveal complex mixtures of secreted proteinsAuthor(s): Amber Vanden Wymelenberg; Patrick Minges; Grzegorz Sabat; Diego Martinez; Andrea Aerts; Asaf Salamov; Igor Grigoriev; Harris Shapiro; Nik Putnam; Paula Belinky; Carlos Dosoretz; Jill Gaskell; Phil Kersten; Dan Cullen
Source: Fungal genetics and biology. Vol. 43 (2006): pages 343-356.
Publication Series: Miscellaneous Publication
PDF: View PDF (1.0 MB)
DescriptionThe white-rot basidiomycete Phanerochaete chrysosporium employs extracellular enzymes to completely degrade the major polymers of wood: cellulose, hemicellulose, and lignin. Analysis of a total of 10,048 v2.1 gene models predicts 769 secreted proteins, a substantial increase over the 268 models identified in the earlier database (v1.0). Within the v2.1 ‘computational secretome,’ 43% showed no significant similarity to known proteins, but were structurally related to other hypothetical protein sequences. In contrast, 53% showed significant similarity to known protein sequences including 87 models assigned to 33 glycoside hydrolase families and 52 sequences distributed among 13 peptidase families. When grown under standard ligninolytic conditions, peptides corresponding to 11 peptidase genes were identified in culture filtrates by mass spectrometry (LS–MS/MS). Five peptidases were members of a large family of aspartyl proteases, many of which were localized to gene clusters. Consistent with a role in dephosphorylation of lignin peroxidase, a mannose-6-phospha-tase (M6Pase) was also identified in carbon-starved cultures. Beyond proteases and M6Pase, 28 specific gene products were identified including several representatives of gene families. These included 4 lignin peroxidases, 3 lipases, 2 carboxylesterases, and 8 glycosyl hydrolases. The results underscore the rich genetic diversity and complexity of P. chrysosporium’s extracellular enzyme systems.
- We recommend that you also print this page and attach it to the printout of the article, to retain the full citation information.
- This article was written and prepared by U.S. Government employees on official time, and is therefore in the public domain.
CitationVanden Wymelenberg, Amber; Minges, Patrick; Sabat, Grzegorz; Martinez, Diego; Aerts, Andrea; Salamov, Asaf; Grigoriev, Igor; Shapiro, Harris; Putnam, Nik; Belinky, Paula; Dosoretz, Carlos; Gaskell, Jill; Kersten, Phil; Cullen, Dan 2006. Computational analysis of the Phanerochaete chrysosporium v2.0 genome database and mass spectrometry identiWcation of peptides in ligninolytic cultures reveal complex mixtures of secreted proteins. Fungal genetics and biology. Vol. 43 (2006): pages 343-356.
KeywordsPhanerochaete chrysosporium, secretion, secretome, proteome, gene cluster, proteins, lignocellulose, hemicellulose, gene expression, Basidiomycetes, wood-decaying fungi, enzymes, mass spectrometry, biodegradation, peptides, genomes, molecular genetics, fungi, industrial applications, wood decay, white rot
- Transcriptome and secretome analyses of Phanerochaete chrysosporium reveal complex patterns of gene expression
- The Phanerochaete chrysosporium secretome : database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium
- Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium
XML: View XML