The 1-Cys peroxiredoxin, a regulator of seed dormancy, functions as a molecular chaperone under oxidative stress conditions

Copyright © 2011 Elsevier Ireland Ltd. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 181(2011), 2 vom: 15. Aug., Seite 119-24
1. Verfasser: Kim, Sun Young (VerfasserIn)
Weitere Verfasser: Paeng, Seol Ki, Nawkar, Ganesh M, Maibam, Punyakishore, Lee, Eun Seon, Kim, Kang-San, Lee, Deok Ho, Park, Dong-Jin, Kang, Sun Bin, Kim, Mi Ri, Lee, Joo Hyeong, Kim, Young Hun, Kim, Woe Yeon, Kang, Chang Ho
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Antioxidants Molecular Chaperones Recombinant Proteins Hydrogen Peroxide BBX060AN9V Peroxiredoxins EC 1.11.1.15 Cysteine K848JZ4886
Beschreibung
Zusammenfassung:Copyright © 2011 Elsevier Ireland Ltd. All rights reserved.
Peroxiredoxins are antioxidative enzymes that catalyze the reduction of alkyl hydroperoxides to alcohols and hydrogen peroxide to water. 1-Cys peroxiredoxins (1-Cys Prxs) perform important roles during late seed development in plants. To characterize their biochemical functions in plants, a 1Cys-Prx gene was cloned from a Chinese cabbage cDNA library and designated as "C1C-Prx". Glutamine synthetase (GS) protection and hydrogen peroxide reduction assays indicated that C1C-Prx was functionally active as a peroxidase. Also C1C-Prx prevented the thermal- or chemical-induced aggregation of malate dehydrogenase and insulin. Hydrogen peroxide treatment changed the mobility of C1C-Prx on a two-dimensional gel, which implies overoxidation of the conserved Cys residue. Furthermore, after overoxidation, the chaperone activity of C1C-Prx increased approximately two-fold, but its peroxidase activity decreased to the basal level of the reaction mixture without enzyme. However, according to the structural analysis using far-UV circular dichroism spectra, intrinsic tryptophan fluorescence spectra, and native-PAGE, overoxidation did not lead to a conformational change in C1C-Prx. Therefore, our results suggest that 1-Cys Prxs function not only to relieve mild oxidative stresses but also as molecular chaperones under severe conditions during seed germination and plant development, and that overoxidation controls the switch in function of 1-Cys-Prxs from peroxidases to molecular chaperones
Beschreibung:Date Completed 16.08.2012
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2011.04.010