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首页> 美国政府科技报告 >Comparative Genomics of Wood Decay Fungi Phanerochaete Chrysosporium and Ceriporiopsis Subvermispora Provides Insight into Mechanisms of Selective Ligninolysis.
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Comparative Genomics of Wood Decay Fungi Phanerochaete Chrysosporium and Ceriporiopsis Subvermispora Provides Insight into Mechanisms of Selective Ligninolysis.

机译：木材腐烂真菌phanerochaete Chrysosporium和Ceriporiopsis subvermispora的比较基因组学提供了对选择性木质素分解机制的深入了解。

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摘要

Efficient lignin depolymerization is unique to the wood decay basidiomycetes collectively referred to as white rot fungi. The model white rot fungus, Phanerochaete chrysosporium, simultaneously degrades lignin and cellulose while the closely related polypore, Ceriporiopsis subvermispora, rapidly depolymerizes lignin with relatively little cellulose degradation. To further our understanding of selective ligninolysis, we report here comparative genome analysis of C. subvermispora and P. chrysosporium. The number, organization, and expression patterns of genes encoding extracellular oxidoreductases varied significantly. Genes encoding manganese peroxidase (MnP) numbered 15 and 5 in C. subvermispora and P. chrysosporium, respectively. The C. subvermispora genome contains at least 7 genes predicted to encode laccases, an observation in distinct contrast to the P. chrysosporium genome which contains none of these multicopper oxidases. When the fungi were grown in media containing ground wood as sole carbon source, mass spectrometry unambiguously identified peptides corresponding to two C. subvermipsora mnp and a laccase genes. We also observed expansion of the number of C. subvermispora genes putatively involved in lipid metabolism and our microarray-based transcriptome analysis showed substantial upregulation of these genes in wood-containing medium. These results support the importance of MnP and a degradation mechanism whereby cleavage of the dominant non-phenolic structures within lignin are mediated by lipid peroxidation products. Beyond the MnPs, two C. subvermispora genes were predicted to encoded peroxidases structurally similar to P. chrysosporium lignin peroxidase (LiP), which have not been reported in C. subvermispora, and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn(II). Quite apart from the oxidative metabolism typically ascribed to lignin degradation, we also considered cellulolytic and hemicellulolytic systems. Overall, the repertoire of glycoside hydrolase-encoding genes was similar in the two species. However, gene expression patterns revealed relatively higher transcript and protein levels in P. chrysosporium suggesting that selective decay by C. subvermispora entails increased oxidative ligninolysis and less active hydrolysis of glycosidic bonds.

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