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

页码：1 / 6

页数：6

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