The Trametes hirsuta 072 laccase multigene family: Genes identification and transcriptional analysis under copper ions induction

• Published in: Biochimie 2015-09, Vol.116, p.154-164
• Main Authors: Vasina, Daria V., Mustafaev, Orkhan N., Moiseenko, Konstantin V., Sadovskaya, Natalia S., Glazunova, Olga A., Tyurin, Аlexander А., Fedorova, Tatiana V., Pavlov, Andrey R., Tyazhelova, Tatiana V., Goldenkova-Pavlova, Irina V., Koroleva, Olga V.
• Format: Article
• Language: English
• Subjects: Copper - pharmacology; Differential expression; Fungal Proteins - genetics; Fungal Proteins - metabolism; Gene Expression Regulation, Fungal - drug effects; Gene Expression Regulation, Fungal - genetics; Laccase - classification; Laccase - genetics; Laccase - metabolism; Laccase multigene family; Multigene Family - genetics; Phylogenetic analysis; Phylogeny; Trametes - drug effects; Trametes - enzymology; Trametes - genetics; White-rot fungi
• ISSN: 0300-9084; 1638-6183
• DOI: 10.1016/j.biochi.2015.07.015

Laccases, blue copper-containing oxidases, ≿an play an important role in a variety of natural processes. The majority of fungal laccases are encoded by multigene families that express closely related proteins with distinct functions. Currently, only the properties of major gene products of the fungal laccase families have been described. Our study is focused on identification and characterization of laccase genes, which are transcribed in basidiomycete Trametes hirsuta 072, an efficient lignin degrader, in a liquid medium, both without and with induction of laccase transcription by copper ions. We carried out production of cDNA libraries from total fungal RNA, followed by suppression subtractive hybridization and mirror orientation selection procedures, and then used Next Generation Sequencing to identify low abundance and differentially expressed laccase transcripts. This approach resulted in description of five laccase genes of the fungal family, which, according to the phylogenetic analysis, belong to distinct clusters within the Trametes genus. Further analysis established similarity of physical, chemical, and catalytic properties between laccases inside each cluster. Structural modeling suggested importance of the sequence differences in the clusters for laccase substrate specificity and catalytic efficiency. The implications of the laccase variations for the fungal physiology are discussed. •Five new laccase genes in Trametes hirsuta were identified and characterized.•Differential transcription of T. hirsuta laccases is observed under copper induction.•Laccases from T. hirsuta belonged to distinct clusters within the Trametes genus.•Clustering of laccases and their role in the physiology of fungi is discussed.