Xenomic networks variability and adaptation traits in wood decaying fungi.
Bottom Line: Taking advantage of the recent release of numerous genomes of basidiomycetes, we show here that these multigenic families are extended and functionally related in wood-decaying fungi.Furthermore, we postulate that these rapidly evolving multigenic families could reflect the adaptation of these fungi to the diversity of their substrate and provide keys to understand their ecology.This is of particular importance for white biotechnology, this xenome being a putative target for improving degradation properties of these fungi in biomass valorization purposes.
Affiliation: Université de Lorraine, IAM, UMR 1136, IFR 110 EFABA, Vandoeuvre-lès-Nancy, F-54506, France. firstname.lastname@example.orgShow MeSH
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Mentions: Soluble GSTs are usually dimeric enzymes, each monomer being composed of two domains. The N-terminal domain, which is more or less conserved, is involved in glutathione binding (G-site). The C-terminal domain is more variable and is involved in the binding of substrates (H-site). The nomenclature of cytosolic GSTs is based on amino acid sequence identity and at least eight classes have been described to date in fungi and named GTT1, GTT2, URE2p, MAK16, EFb1, Etherase-like recently renamed GSTFuA (Mathieu et al., 2012), GSTO and GHR (McGoldrick et al., 2005, Morel et al., 2009) (Fig. 2). Traditionally, two proteins belong to the same class if they share more than 40% identity and isoenzymes belonging to different classes share less than 20% (Hayes et al., 2005). Nevertheless, based on these primary sequence criteria only, many ‘non-canonical’ GST groups have emerged especially in bacteria and fungi, increasing the complexity of the GSTs classification. A few protein families are usually classified as GSTs (EF1Bγ, MAK16), but this is rather based on structural similarities, not on the existence of a glutathione-dependent activity. In addition, further immunologic, genetic, structural and functional investigations could reveal unexpected similarities between enzymes first listed in different groups (Meux et al., 2012). This emphasizes the challenge of GST classification.
Affiliation: Université de Lorraine, IAM, UMR 1136, IFR 110 EFABA, Vandoeuvre-lès-Nancy, F-54506, France. email@example.com