Differential roles of glutathione S-transferases in oxidative stress
Clatot, N.
Glutathione S-transferases (GSTs) are a diverse family of dimeric proteins found in almost all living organisms. Originally studied for their role in detoxification of endogenous and xenobiotic compounds, they have since been found to have additional important roles as transport proteins and in protection against oxidative stress. The present study focuses on the biochemical characterization of two GST classes, the Omega class and the Tau class. GST Omega is a new class of GSTs discovered by the Gabel and Board group in the year 2000. This class of GST has shown new features not seen before in the other GSTs, like glutaredoxin-like activities and an active site cysteine. Some studies led to the discovery of new functions for the GSTO: as a regulator of intracellular [Ca sup(2+)], as a protector of cells containing RyR2, as a MonoMethylarsenic Acid reductase, and most recently, as a CRID (Cytokine Release Inhibitory Drug) binding protein. The Tau class of glutathione S-transferases is plant specific. In a recent study, five Tau-class proteins from tomato have been isolated as interactors of BI-GST. The study primarily focused on the kinetics of LeGSTU3 protein using the most common GST substrate CDNB. A cooperativity mechanism was found when the GSH concentration varied. The limited proteolysis of LeGSTU2 and LeGSTU3 showed different proteolytic patterns for these two proteins, despite their homology.
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