Genome-wide analysis of the Pleurotus eryngii laccase gene (PeLac) family and functional identification of PeLac5.

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.