Hsp104 and ClpB: protein disaggregating machines

被引：214

作者：

Doyle, Shannon M. ^{[1
]}

Wickner, Sue ^{[1
]}

机构：

[1] NCI, Mol Biol Lab, NIH, Bethesda, MD 20892 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2009年 / 34卷 / 01期

基金：

美国国家卫生研究院;

关键词：

PLUS CHAPERONE CLPB; SACCHAROMYCES-CEREVISIAE HSP104; TERMINAL ATPASE DOMAIN; ESCHERICHIA-COLI; MOLECULAR CHAPERONE; DEGRADATION MACHINE; SUBSTRATE RECOGNITION; AGGREGATED PROTEINS; NUCLEOTIDE-BINDING; PRION PROPAGATION;

D O I：

10.1016/j.tibs.2008.09.010

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：

Heat-shock protein 104 (Hsp104) and caseinolytic peptidase B (ClpB), members of the AAA+ superfamily, are molecular machines involved in disaggregating insoluble protein aggregates, a process not long ago thought to be impossible. During extreme stress they are essential for cell survival. In addition, Hsp104 regulates prion assembly and disassembly. For most of their protein remodeling activities Hsp104 and ClpB work in collaboration with the Hsp70 or DnaK chaperone systems. Together, the two chaperones catalyze protein disaggregation and reactivation by a mechanism probably involving the extraction of polypeptides from aggregates by forced unfolding and translocation through the Hsp104/ClpB central cavity. The polypeptides are then released back into the cellular milieu for spontaneous or chaperone-mediated refolding.

引用

页码：40 / 48

页数：9

共 81 条

[1] Site-directed mutagenesis of conserved charged amino acid residues in C1pβ from Escherichia coli [J].