Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes

Mathieu Schwartz (1) , Thomas Perrot (2) , Aurélie Deroy (2) , Thomas Roret (3) , Melanie Morel-Rouhier (2) , Guillermo Mulliert (1) , Éric Gelhaye (2) , Frédérique Favier (1) , Claude Didierjean (1)

1 UL - Université de Lorraine
2 IAM - Interactions Arbres-Microorganismes
3 SU - Sorbonne Université

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.

Mots clés: crystallography; dual enzyme activity; glutathione transferase Xi; glutathionyl-acetophenone reductase; glutathionyl-hydroquinone reductase; HYDROQUINONE REDUCTASES; S-GLUTATHIONYL-(CHLORO)HYDROQUINONE REDUCTASES; POPULUS-TRICHOCARPA; S-TRANSFERASES; PLANTS; REDUCTION; IDENTIFICATION; MECHANISM; INSIGHTS; GENES

Mots clés: gluthatione s transférase; résidu cystéine; champignon saprophyte; champignon ascomycete; trametes versicolor

Domaines: Sciences du Vivant [q-bio]

Mathieu Schwartz, Thomas Perrot, Aurélie Deroy, Thomas Roret, Melanie Morel-Rouhier, et al.. Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes. FEBS Letters, 2018, 592 (18), pp.3163-3172. ⟨10.1002/1873-3468.13224⟩. ⟨hal-01959634⟩