Abstract
Glutathione S-transferases (GSTs) are dimeric multifunctional enzymes catalyzing the nucleophilic attack of the thiol group of glutathione forming conjugates with various electrophilic substrates. GSTs are present in all plant tissues and at all stages of plant development from early embryogenesis to senescence. An established role of plant GSTs is their involvement in herbicide detoxification. Plant GSTs have also been implicated in defense mechanisms against other stress responses such as pathogenic attack, oxidative stress, heavy-metal toxicity and the cellular response to auxins and the normal metabolism of secondary plant products such as anthocyanins and cinnamic acid. Plant GSTs are characterized and differentiated by broad and partial overlapping substrate specificity, heterogeneity of subunit composition and amino acid sequences, and differential regulation by herbicide safeners. The safener-mediated regulation of plant GSTs appears to be a stepwise process, requiring signal transduction from putative safener receptors to other cellular sites.
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