Abstract
BackgroundGlutathione S-transferases (GSTs) are the ubiquitous enzymes that play a key role in cellular detoxification. Although several GSTs have been identified and characterized in various plant species, the knowledge about their role in developmental processes and response to various stimuli is still very limited. In this study, we report genome-wide identification, characterization and comprehensive expression analysis of members of GST gene family in crop plant rice, to reveal their function(s).ResultsA systematic analysis revealed the presence of at least 79 GST genes in the rice genome. Phylogenetic analysis grouped GST proteins into seven classes. Sequence analysis together with the organization of putative motifs indicated the potential diverse functions of GST gene family members in rice. The tandem gene duplications have contributed a major role in expansion of this gene family. Microarray data analysis revealed tissue-/organ- and developmental stage-specific expression patterns of several rice GST genes. At least 31 GST genes showed response to plant hormones auxin and cytokinin. Furthermore, expression analysis showed the differential expression of quite a large number of GST genes during various abiotic stress (20), arsenate stress (32) and biotic stress (48) conditions. Many of the GST genes were commonly regulated by developmental processes, hormones, abiotic and biotic stresses.ConclusionThe transcript profiling suggests overlapping and specific role(s) of GSTs during various stages of development in rice. Further, the study provides evidence for the role of GSTs in mediating crosstalk between various stress and hormone response pathways and represents a very useful resource for functional analysis of selected members of this family in rice.
Highlights
Glutathione S-transferases (GSTs) are the ubiquitous enzymes that play a key role in cellular detoxification
Glutathione transferases (GSTs, EC 2.5.1.18), formerly known as glutathione S-transferases, are the enzymes involved in cellular detoxification by conjugating the tripeptide (g-Glu-Cys-Gly) glutathione (GSH) to a wide variety of substrates such as endobiotic and xenobiotic compounds [1]
Based on the predicted amino acid sequences, the soluble GSTs in plants have been grouped into several classes, including Phi, Tau, Lambda, dehydroascorbate reductase (DHAR), Theta, Zeta, elongation factor 1 gamma (EF1G) and tetrachlorohydroquinone dehalogenase (TCHQD)
Summary
Glutathione S-transferases (GSTs) are the ubiquitous enzymes that play a key role in cellular detoxification. GSTs have been identified in all the organisms, including plants, animals, fungi and bacteria analyzed to date [2,3]. Several GSTs have been identified and characterized in various plant species with differential and overlapping substrate specificities [5,8,9]. Based on the predicted amino acid sequences, the soluble GSTs in plants have been grouped into several classes, including Phi, Tau, Lambda, dehydroascorbate reductase (DHAR), Theta, Zeta, elongation factor 1 gamma (EF1G) and tetrachlorohydroquinone dehalogenase (TCHQD). Among these classes, Phi, Tau, Lambda and DHAR classes are plant specific [10]
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