Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes
2018
Schwartz, Mathieu | Perrot, Thomas | Deroy, Aurélie | Roret, Thomas | Morel-Rouhier, Melanie | Mulliert, Guillermo | Gelhaye, Éric | Favier, Frédérique | Didierjean, Claude | Université de Lorraine (UL) | Interactions Arbres-Microorganismes (IAM) ; Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL) | Sorbonne Université (SU) | Laboratory of Excellence Advanced Research on the Biology of Tree and Forest Ecosystems (ARBRE grant) ANR 11 LABX 0002 01 ; 'Impact Biomolecules' project of the 'Lorraine Universite d'Excellence' (Investissements d'avenir - ANR) | ANR-11-LABX-0002,ARBRE,Recherches Avancées sur l'Arbre et les Ecosytèmes Forestiers(2011)
Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue, which gives them reductase activities.Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here, we present the biochemical and structural analysis of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected, while TvGSTX3 reduces both Xi and Omega substrates. An in-depth structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix α9.This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis, we propose that this duality might exist in saprophytic fungi and ascomycetes.
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