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Roodgar, Mitra, Shahpiri, Azar. (1395). Replacement of threonine-55 with glycine decreases the reduction rate of OsTrx20 by glutathione. , 6(1), 33-40. doi: 10.22099/mbrc.2017.4001
Mitra Roodgar; Azar Shahpiri. "Replacement of threonine-55 with glycine decreases the reduction rate of OsTrx20 by glutathione". , 6, 1, 1395, 33-40. doi: 10.22099/mbrc.2017.4001
Roodgar, Mitra, Shahpiri, Azar. (1395). 'Replacement of threonine-55 with glycine decreases the reduction rate of OsTrx20 by glutathione', , 6(1), pp. 33-40. doi: 10.22099/mbrc.2017.4001
Roodgar, Mitra, Shahpiri, Azar. Replacement of threonine-55 with glycine decreases the reduction rate of OsTrx20 by glutathione. , 1395; 6(1): 33-40. doi: 10.22099/mbrc.2017.4001

Replacement of threonine-55 with glycine decreases the reduction rate of OsTrx20 by glutathione

Molecular Biology Research Communications
مقاله 5، دوره 6، شماره 1، 2017، صفحه 33-40    اصل مقاله (368.22 K)
نوع مقاله: Original article
شناسه دیجیتال (DOI): 10.22099/mbrc.2017.4001
نویسندگان
Mitra Roodgar؛ Azar Shahpiri*
Department of Biotechnology, College of Agriculture, Isfahan University of ‎Technology, Isfahan, Iran.‎
چکیده
Thioredoxins (Trxs) are small ubiquitous oxidoreductase proteins with two redox-active Cys residues in a conserved active site (WCG/PPC) that regulate numerous target proteins via thiol/disulfide exchanges in the cells of prokaryotes and eukaryotes. The isoforms OsTrx23 with a typical active site (WCGPC) and OsTrx20 with an atypical active site (WCTPC) are two  Trx h- type isoforms in rice that were previously found to be reduced by NADPH-dependent thioredoxin reductase and GSH/Grx system, respectively. In the present work the reduction of mutants G41TOsTrx23, T55GOsTrx20, K48DOsTrx20 and T55G-K48D OsTrx20 as well as wild types OsTrx23 and OsTrx20 were tested in the reaction containing either NADPH/NTR or glutathione (GSH). The results revealed that reduction rate of T55GOsTrx20 was remarkably decreased by GSH as compared to WtOsTrx20 highlighting the critical role of Thr-55 in interaction of OsTrx20 with GSH. On the other hand a significant decrease in the reduction rate of G41TOsTrx23 was observed in reaction containing NADPH-dependent thioredoxin reductase as compared with readuction rate of WtOsTrx23. These results suggest that first residue after N-terminal active site Cys is one of the critical residue in determination of system that Trxs can be reduced in.
کلیدواژه‌ها
Glutathione؛ NADPH-dependent thioredoxin reductase؛ Rice؛ Thioredoxin
مراجع

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