On the path to the heat shock response: Destabilization and formation of partially folded protein intermediates, a consequence of protein thiol modification

被引:86
作者
Freeman, ML
Borrelli, MJ
Meredith, MJ
Lepock, JR
机构
[1] Vanderbilt Univ, Dept Radiat Oncol, Sch Med, Vanderbilt Canc Ctr, Nashville, TN 37232 USA
[2] William Beaumont Hosp, Dept Radiat Oncol, Royal Oak, MI USA
[3] Oregon Hlth & Sci Univ, Sch Dent, Dept Oral Mol Biol, Portland, OR 97201 USA
[4] Univ Waterloo, Dept Biol, Waterloo, ON N2L 3G1, Canada
[5] Univ Waterloo, Dept Phys, Waterloo, ON N2L 3G1, Canada
关键词
free radical; heat shock proteins; protein denaturation; molten globule-like intermediates; Hsf-1; glutathione;
D O I
10.1016/S0891-5849(98)00258-5
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
This review discusses the initial events that occur during oxidative stress that induce the synthesis of heat shock proteins. The focus is on non-native oxidation or modification of protein thiols and the destablization that can result. Proteins that contain non-native modified thiols can become destablized such that they unfold into molten globule-like intermediates at or below 37 degrees C, relieving Hsf-1 negative regulation, and inducing Hsp transcription. (C) 1999 Elsevier Science Inc.
引用
收藏
页码:737 / 745
页数:9
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