Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5905460 | Gene | 2015 | 8 Pages |
Abstract
Fungal laccases play important roles in matrix degradation. Eleven laccase genes, including three novel ones (designated lac1, lac2 and lac4) were identified after sequencing the entire genome of the edible, white-rot fungus Flammulina velutipes. Analysis using bioinformatics revealed that all of the laccases, except lac3, possess a signal peptide. These laccase proteins consist of 502-670 amino acids and have predicted molecular weights ranging from 55Â kDa to 74Â kDa. These proteins each contain four copper-binding sites, except for Lac10. Transcriptomes were sequenced at different developmental stages and in different fruiting body tissues to analyze if there was differential expression of laccase genes. The novel laccase gene lac4 exhibited the highest expression levels among all of the observed laccases at every developmental stage and in all fruiting body tissues examined. We conclude that laccases in F. velutipes play a role not only in lignin degradation, but also in fruiting body formation and development.
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Biochemistry, Genetics and Molecular Biology
Genetics
Authors
Wei Wang, Fang Liu, Yuji Jiang, Guangmei Wu, Lixian Guo, Renliang Chen, Bingzhi Chen, Yuanping Lu, Yucheng Dai, Baogui Xie,