Oxidation-Induced Conformational Change of a Prokaryotic Molecular Chaperone, Hsp33, Monitored by Selective Isotope Labeling

被引：3

作者：

Lee, Yoo-Sup ^{[1
]}

Ryu, Kyoung-Seok ^{[2
]}

Lee, Yuno ^{[3
]}

Kim, Songmi ^{[3
]}

Lee, Keun Woo ^{[3
]}

Won, Hyung-Sik ^{[1
]}

机构：

[1] Konkuk Univ, Dept Biotechnol, Chungju 380701, Chungbuk, South Korea

[2] Korea Basic Sci Inst, Div Magnet Resonance, Ochang, Chungbuk, South Korea

[3] Gyeongsang Natl Univ, PMBBRC, SSAC, Res Inst Nat Sci,Div Appl Life Sci BK21 Program, Jinju 660701, South Korea

来源：

JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY | 2011年 / 15卷 / 02期

基金：

新加坡国家研究基金会;

关键词：

Hsp33; chaperone; selective isotope labeling; conformational change;

D O I：

10.6564/JKMRS.2011.15.2.137

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Hsp33, a prokaryotic molecular chaperone, exerts holdase activity in response to oxidative stress. In this study, the stepwise conformational change of Hsp33 upon oxidation was monitored by NMR. In order to overcome its high molecular weight (33 kDa as a monomer and 66 kDa as a dimer), spectra were simplified using a selectively [N-15] His-labeled protein. All of the eight histidines were observed in the TROSY spectrum of the reduced Hsp33. Among them, three peaks showed dramatic resonance shifts dependent on the stepwise oxidation, indicating a remarkable conformational change. The results suggest that unfolding of the linker domain is associated with dimerization, but not entire region of the linker domain is unfolded.

引用

页码：137 / 145

页数：9

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