Abstract
Glutathione transferases (GSTs) belong to a ubiquitous multigenic family of enzymes involved in diverse biological processes including xenobiotic detoxification and secondary metabolism. A canonical GST is formed by two domains, the N-terminal one adopting a thioredoxin (TRX) fold and the C-terminal one an all-helical structure. The most recent genomic and phylogenetic analysis based on this domain organization allowed the classification of the GST family into 14 classes in terrestrial plants. These GSTs are further distinguished based on the presence of the ancestral cysteine (Cys-GSTs) present in TRX family proteins or on its substitution by a serine (Ser-GSTs). Cys-GSTs catalyze the reduction of dehydroascorbate and deglutathionylation reactions whereas Ser-GSTs catalyze glutathione conjugation reactions and eventually have peroxidase activity, both activities being important for stress tolerance or herbicide detoxification. Through non-catalytic, so-called ligandin properties, numerous plant GSTs also participate in the binding and transport of small heterocyclic ligands such as flavonoids including anthocyanins, and polyphenols. So far, this function has likely been underestimated compared to the other documented roles of GSTs. In this review, we compiled data concerning the known enzymatic and structural properties as well as the biochemical and physiological functions associated to plant GSTs having a conserved serine in their active site.
Highlights
Glutathione transferases (GSTs), formerly glutathione S-transferases, constitute a ubiquitous multigenic superfamily of enzymes that conjugate the tripeptide glutathione (γ-Glu-Cys-Gly) on a broad range of molecules
In a second stage of analysis, we examined the expression profile of these same 44 Ser-GSTs in response to a number of abiotic stresses [AtGenExpress Stress Set; (Kilian et al, 2007)]
The GST gene family was subject to a huge genetic expansion in terrestrial plants, with an average number of GSTs around
Summary
Glutathione transferases (GSTs), formerly glutathione S-transferases, constitute a ubiquitous multigenic superfamily of enzymes that conjugate the tripeptide glutathione (γ-Glu-Cys-Gly) on a broad range of molecules. They catalyze the nucleophilic attack of reduced glutathione (GSH) on the electrophilic centers of these molecules. The omnipresence of these enzymes in all types of organisms highlights an ancient origin as well as fundamental functions preserved during evolution. GHRs are involved in the catabolism of chlorinated quinones and in lignin degradation through the deglutathionylation of metabolic intermediates (Reddy and Gold, 2001; Masai et al, 2003; Huang et al, 2008; Meux et al, 2011)
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