![]() ![]() The protein structure analysis confirmed the occurrence of conserved pyridine nucleotide disulfide oxidoreductase (Pyr_redox) and pyridine nucleotide disulfide oxidoreductase dimerization (Pyr_redox_dim) domains in each GR. The exon–intron and conserved motif patterns were almost conserved in each group, in which a maximum of 10 and 17 exons were present in chloroplastic and cytoplasmic GRs, respectively. Phylogenetic analysis revealed the clustering of GR proteins into two groups class I and class II, which were predicted to be localized in cytoplasm and chloroplast, respectively. ![]() Besides, we identified three GR genes in each Aegilops tauschii, Brachypodium distachyon, Triticum urartu and Sorghum bicolor, which were used for comparative characterization. In this study, a total of seven GR genes forming two homeologous groups were identified in the allohexaploid genome of bread wheat ( Triticum aestivum). Glutathione reductase (GR) is an enzymatic antioxidant that converts oxidized glutathione (GSSG) into reduced glutathione (GSH) through the ascorbate–glutathione cycle. The modulated gene expression and enzyme activity revealed the role of GRs in abiotic stress response in T. A total of seven glutathione reductase ( GR) genes were identified in Triticum aestivum, which were used for comparative structural characterization, phylogenetic analysis and expression profiling with the GR genes of other cereal plants.
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