AUTHOR=Xu Lili , Yang Wujie , Qiu Tianmei , Gao Xia , Zhang Hongyong , Zhang Shuliang , Cui Hui , Guo Lizhong , Yu Hailong , Yu Hao 

TITLE=Complete genome sequences and comparative secretomic analysis for the industrially cultivated edible mushroom Lyophyllum decastes reveals insights on evolution and lignocellulose degradation potential

JOURNAL=Frontiers in Microbiology

VOLUME=14

YEAR=2023

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2023.1137162

DOI=10.3389/fmicb.2023.1137162

ISSN=1664-302X

ABSTRACT=<p><italic>Lyophyllum decastes</italic>, also known as Luronggu in China, is a culinary edible and medicinal mushroom that was widely cultivated in China in recent years. In the present study, the complete high-quality genome of two mating compatible <italic>L. decastes</italic> strain was sequenced. The <italic>L. decastes</italic> LRG-d1-1 genome consists of 47.7 Mb in 15 contigs with a contig N90 of 2.08 Mb and 14,499 predicted gene models. Phylogenetic analysis revealed that <italic>L. decastes</italic> exhibits a close evolutionary relationship to the <italic>Termitomyces</italic> and <italic>Hypsizygus</italic> genus and was diverged from <italic>H. marmoreus</italic>  ~ 45.53 Mya ago. Mating <italic>A</italic> loci of <italic>L. decastes</italic> compose of five and four <italic>HD</italic> genes in two monokaryotic strains, respectively. Mating <italic>B</italic> loci compose of five <italic>STE</italic> genes in both two monokaryotic strains. To accelerate the cross-breeding process, we designed four pairs of specific primers and successfully detected both mating types in <italic>L. decastes</italic>. As a wood-rotting mushroom, a total of 541 genes accounting for 577 CAZymes were identified in the genome of <italic>L. decastes</italic>. Proteomic analysis revealed that 1,071 proteins including 182 CAZymes and 258 secreted enzymes were identified from four groups (PDB, PDB + bran, PDB + cotton hull, and PDB + sawdust). Two laccases and a quinone reductase were strongly overproduced in lignin-rich cultures, and the laccases were among the top-3 secreted proteins, suggesting an important role in the synergistic decomposition of lignin. These results revealed the robustness of the lignocellulose degradation capacity of <italic>L. decastes</italic>. This is the first study to provide insights into the evolution and lignocellulose degradation of <italic>L. decastes</italic>.</p>