Oligomerization and chaperone activity of a plant 2-Cys peroxiredoxin in response to oxidative stress |
| |
Authors: | Sun Young Kim Ho Hee Jang Jung Ro Lee Nu Ri Sung Hae Bin Lee Deok Ho Lee Dong-Jin Park Chang Ho Kang Woo Sik Chung Chae Oh Lim Dae-Jin Yun Woe Yeon Kim Kyun Oh Lee Sang Yeol Lee |
| |
Affiliation: | 1. Environmental Biotechnology National Core Research Center, PMBBRC, Division of Applied Life Sciences (BK21 Program), Gyeongsang National University, Jinju, 660-701, Republic of Korea;2. Lee Gil Ya Cancer & Diabetes Institute, Gachon University of Medicine & Science, Gachon, Republic of Korea |
| |
Abstract: | Plant 2-Cys peroxiredoxins (2-Cys Prxs) have been reported to localize to chloroplasts and perform antioxidative roles during plant development and photosynthesis. In this study, we identified that, in addition to the well-known function of thioredoxin (Trx)-dependent peroxidase, the plant 2-Cys Prx in Chinese cabbage 2-Cys Prx1, designated C2C-Prx1, also behaves as a molecular chaperone under oxidative stress conditions, like the yeast and mammalian 2-Cys Prxs. By the chaperone function of C2C-Prx1, the protein efficiently prevented the denaturation of citrate synthase and insulin from heat shock and dithiothreitol (DTT)-induced chemical stresses. Also, the protein structure of C2C-Prx1 was shown to have discretely sized multiple structures, whose molecular sizes were in the diverse ranges of low molecular weight (LMW) proteins to high molecular weight (HMW) protein complexes. The dual functions of C2C-Prx1 acting as a peroxidase and as a molecular chaperone are alternatively switched by heat shock and oxidative stresses, accompanying with its structural changes. The peroxidase function predominates in the lower MW forms, but the chaperone function predominates in the higher MW complexes. The precise regulation of C2C-Prx1 structures and functions may play a pivotal role in the protection of plant chloroplasts from photo-oxidative stress. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|