Aggregate reactivation mediated by the Hsp100 chaperones

被引：53
|
作者：
Zolkiewski, Michal [1 ]
Zhang, Ting [1 ]
Nagy, Maria [2 ]
机构：
[1] Kansas State Univ, Dept Biochem, Manhattan, KS 66506 USA
[2] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA
来源：
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2012年 / 520卷 / 01期
基金：
美国国家卫生研究院;
关键词：
Protein aggregation; Aggregate reactivation; Molecular chaperone; ClpB; Hsp104; AAA plus ATPase; UBIQUITIN-PROTEASOME SYSTEM; AMINO-TERMINAL DOMAIN; HEAT-SHOCK PROTEINS; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; SACCHAROMYCES-CEREVISIAE; MOLECULAR CHAPERONES; HUNTINGTONS-DISEASE; STRESS TOLERANCE; QUALITY-CONTROL;
D O I：
10.1016/j.abb.2012.01.012
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：
Hsp100 family of molecular chaperones shows a unique capability to resolubilize and reactivate aggregated proteins. The Hsp100-mediated protein disaggregation is linked to the activity of other chaperones from the Hsp70 and Hsp40 families. The best-studied members of the Hsp100 family are the bacterial ClpB and Hsp104 from yeast. Hsp100 chaperones are members of a large super-family of energy-driven conformational "machines" known as AAA+ ATPases. This review describes the current mechanistic model of the chaperone-induced protein disaggregation and explains how the structural architecture of Hsp100 supports disaggregation and how the co-chaperones may participate in the Hsp100-mediated reactions. (C) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码：1 / 6
页数：6
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