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Structure, Organization, and Transcriptional Regulation of a Family of Copper Radical Oxidase Genes in the Lignin-Degrading

By Basidiomycete Phanerochaete Chrysosporium, Amber V, En Wymelenberg, Grzegorz Sabat, Michael Mozuch, Philip J. Kersten, Dan Cullen and Robert A. Blanchette

Abstract

The white rot basidiomycete Phanerochaete chrysosporium produces an array of nonspecific extracellular enzymes thought to be involved in lignin degradation, including lignin peroxidases, manganese peroxidases, and the H 2O 2-generating copper radical oxidase, glyoxal oxidase (GLX). Preliminary analysis of the P. chrysosporium draft genome had identified six sequences with significant similarity to GLX and designated cro1 through cro6. The predicted mature protein sequences diverge substantially from one another, but the residues coordinating copper and constituting the radical redox site are conserved. Transcript profiles, microscopic examination, and lignin analysis of inoculated thin wood sections are consistent with differential regulation as decay advances. The cro2-encoded protein was detected by liquid chromatography-tandem mass spectrometry in defined medium. The cro2 cDNA was successfully expressed in Aspergillus nidulans under the control of the A. niger glucoamylase promoter and secretion signal. The recombinant CRO2 protein had a substantially different substrate preference than GLX. The role of structurally and functionally diverse cro genes in lignocellulose degradation remains to be established. The most abundant source of global carbon is plant biomass composed primarily of cellulose, hemicellulose, and lignin. White rot basidiomycetes, such as Phanerochaete chrysosporium

Year: 2006
OAI identifier: oai:CiteSeerX.psu:10.1.1.328.6529
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