期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 179, 期 2, 页码 161-171出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2012.05.015
关键词
AAA plus -ATPase; Molecular chaperone; Hsp100; ClpB; Hsp104; Allostery
资金
- Biotechnology and Biological Sciences Research Council (UK) [BB/G01468X/1]
- BBSRC [BB/G01468X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G01468X/1] Funding Source: researchfish
The AAA.-ATPases are a family of molecular motors which have been seconded into a plethora of cellular tasks. One subset, the Hsp100 molecular chaperones, are general protein remodellers that help to maintain the integrity of the cellular proteome by means of protein destruction or resurrection. In this review we focus on one family of Hsp100s, the homologous ClpB and Hsp104 molecular chaperones that convey thermotolerance by resolubilising and rescuing proteins from aggregates. We explore how the nucleotide binding and hydrolysis properties at the twelve nucleotide-binding domains of these hexameric rings are coupled to protein disaggregation, highlighting similarities and differences between ClpB and Hsp104. (C) 2012 Elsevier Inc. All rights reserved.
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