Redox properties of the A-domain of the HMGB1 protein

被引：42

作者：

Sahu, Debashish ^{[1
]}

Debnath, Priyanka ^{[1
]}

Takayama, Yuki ^{[1
]}

Iwahara, Junji ^{[1
]}

机构：

[1] Univ Texas Med Branch, Sealy Ctr Struct Biol & Mol Biophys, Dept Biochem & Mol Biol, Galveston, TX 77555 USA

来源：

FEBS LETTERS | 2008年 / 582卷 / 29期

关键词：

HMGB1; Redox; Disulfide bond; Thermodynamics; Kinetics; NMR spectroscopy;

D O I：

10.1016/j.febslet.2008.09.061

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The High Mobility Group B1 (HMGB1) protein plays important roles in both intracellular (reductive) and extracellular (oxidative) environments. We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond. Using NMR spectroscopy, we analyzed the realtime kinetics of the redox reactions for the A-domain in glutathione and thioredoxin systems, and also determined the standard redox potential. Thermodynamic experiments showed that the Cys22-Cys44 disulfide bond stabilizes the folded state of the protein. These data suggest that the oxidized HMGB1 may accumulate even in cells under oxidative stress.

引用

页码：3973 / 3978

页数：6

共 17 条

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