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Genome-wide analysis of the Pleurotus eryngii laccase gene (PeLac) family and functional identification of PeLac5
Original Article
Congtao Xu1  Yi Zhou1  Yuanyuan Zhou1  Zihao Li1  Jinlong Pan1  Yajie Zou1  Haikang Li1 
[1] State Key Laboratory of Efficient Utilization of Arid and Semi-arid Arable Land in Northern China, 100081, Beijing, China;Institute of Agricultural Resources and Regional Planning, Chinese Academy of Agricultural Sciences, 100081, Beijing, China;
关键词: Pleurotus eryngii;    Laccase;    Genome-wide profiling;    Expression pattern;    Lignocellulose degradation;   
DOI  :  10.1186/s13568-023-01608-w
 received in 2023-09-01, accepted in 2023-09-12,  发布年份 2023
来源: Springer
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【 摘 要 】

The laccase gene family encodes multiple isozymes that are crucial for the degradation of substrates and the regulation of developmental processes in fungi. Pleurotus eryngii is an important edible and medicinal fungus belonging to the Basidiomycota phylum and can grow on a variety of natural substrates. In the present study, genome-wide profiling of P. eryngii identified 10 genes encoding its laccase isoenzymes. Conservative sequence analysis demonstrated that all PeLacs possess classical laccase structural domains. Phylogenetic analysis yielded four major subgroups, the members of which are similar with respect to conserved gene organization, protein domain architecture, and consensus motifs. The 10 PeLacs formed three groups together with 12 PoLacs in Pleurotus ostreatus, indicating that they share a high level of evolutionary homology. Cis-responsive element analysis implied that PeLacs genes play a role in growth and development and lignocellulose degradation. Targeted overexpression of PeLac5 reduced the time to primordia formation and their development to fruiting bodies. Gene expression patterns in the presence of different lignocellulosic substrates indicate that three PeLacs genes (2, 4, and 9) are key to lignocellulose degradation. This work presents the first inventory of laccase genes in P. eryngii and preliminarily explores their functions, which may help to uncover the manner by which these proteins utilize substrates.

【 授权许可】

CC BY   
© Springer-Verlag GmbH Germany, part of Springer Nature 2023

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