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

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• 作者：Sun Young Kim^a ; Seol Ki Paeng^a ; Ganesh M. Nawkar^a ; Punyakishore Maibam^a ; Eun Seon Lee^a ; Kang-San Kim^a ; Deok Ho Lee^a ; Dong-Jin Park^a ; Sun Bin Kang^a ; Mi Ri Kim^a ; Joo Hyeong Lee^b ; Young Hun Kim^a ; Woe Yeon Kim^a ; ^{kim1312@gnu.ac.kr"" rel=""nofollow} ; Chang Ho Kang^a ; ^{jacobgnu69@gnu.ac.kr"" rel=""nofollow}
• 关键词：Chaperone ; Plant 1-Cys peroxiredoxin ; Peroxiredoxin ; Overoxidation
• 刊名：Plant Science
• 出版年：2011
• 出版时间：August 2011
• 年：2011
• 卷：181
• 期：2
• 页码：119-124
• 全文大小：991 K

文摘

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.