A new member of Tau-class glutathione S-transferase from barley leaves

Abstract

Glutathione S-transferase is a family of multifunctional detoxification enzymes which are mainly cytosolic that detoxify natural and exogenous toxic compounds by conjugation with glutathione. Glutathione, an endogenous tripeptide, is important as either a reducing agent or a nucleophilic scavenger. This molecule alleviates the chemical toxicity in plants by reaction of glutathione S-transferase, and its conjugates can be transported to vacuole or apoplast. The plant soluble glutathione S-transferases grouped today into seven distinct Phi, Tau, Zeta, Theta, lambda, dehydroascorbate reductase, and tetrachlorohydroquinone dehalogenase classes. In this study, bioinformatics analysis of glutathione S-transferase gene in barley was carried out using Tau-class of barley glutathione S-transferase sequences in NCBI GenBank and isolated sequence. DNA extraction, primer design, PCR, electrophoresis, column purification, DNA sequencing and analysis by some software led to identify new sequences of Tauclass of glutathione S-transferase from barley, which is similar to Tau GST of the diploid wheat. Comparison of the deduced amino acid sequences of the three barley GST genes showed that they have 99 % identity with each other but only 45 % identity with the new GST. This sequence was submitted to NCBI GenBank with FI131240 accession number.