Skip to page content
USDA Forest Service
  
Treesearch

Research & Development Treesearch

 
Treesearch Home
About Treesearch
Contact Us
Research & Development
Forest Products Lab
International Institute of Tropical Forestry
Northern
Pacific Northwest
Pacific Southwest
Rocky Mountain
Southern Research Station
Help
 

Science.gov - We Participate


USA.gov  Government Made Easy


Global Forest Information Service

US Forest Service
P.O. Box 96090
Washington, D.C.
20090-6090

(202) 205-8333

You are here: Home / Search / Publication Information
Bookmark and Share

Publication Information

View PDF (1.0 MB byte)

Title: 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

Author: Vanden 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;

Date: 2006

Source: Fungal genetics and biology. Vol. 43 (2006): pages 343-356.

Publication Series: Miscellaneous Publication

Description: The 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.

Keywords: Phanerochaete 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

Publication Notes:

  • 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.

XML: View XML

Citation:


Vanden 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.

 


 [ Get Acrobat ]  Get the latest version of the Adobe Acrobat reader or Acrobat Reader for Windows with Search and Accessibility

USDA logo which links to the department's national site. Forest Service logo which links to the agency's national site.