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PMID: 24026055 Published · ppublish English Journal Article Review

Chaperone machines for protein folding, unfolding and disaggregation.

Nature reviews. Molecular cell biology ·Vol. 14 ·No. 10 ·2013-10-00 ·Pages 630-42

Saibil H

Abstract

Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascent proteins to reach their native fold, protect subunits from heat shock during the assembly of complexes, prevent protein aggregation or mediate targeted unfolding and disassembly. Their increased expression in response to stress is a key factor in the health of the cell and longevity of an organism. Unlike enzymes with their precise and finely tuned active sites, chaperones are heavy-duty molecular machines that operate on a wide range of substrates. The structural basis of their mechanism of action is being unravelled (in particular for the heat shock proteins HSP60, HSP70, HSP90 and HSP100) and typically involves massive displacements of 20-30 kDa domains over distances of 20-50 Å and rotations of up to 100°.

MeSH Terms
HSP70 Heat-Shock Proteins/chemistry,metabolism HSP90 Heat-Shock Proteins/chemistry,metabolism Heat-Shock Response/genetics,physiology Humans Molecular Chaperones/chemistry,metabolism Protein Conformation Protein Folding Protein Structure, Quaternary Protein Unfolding Quality Control
Chemicals
HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Molecular Chaperones
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Saibil Helen
Department of Crystallography, Institute for Structural and Molecular Biology, Birkbeck College London, UK.
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Article Info
Journal
Nature reviews. Molecular cell biology
Abbr.
Nat Rev Mol Cell Biol
ISSN
1471-0080
DOI
10.1038/nrm3658
Published
2013-10-00
Epub
2013-00-12
Pages
630-42
Language
English
Region
England
NLM ID
100962782
PMCID
PMC4340576
Subset
IM
Grants
Wellcome Trust · 070776 · United Kingdom
External Links
PubMed source DOI: 10.1038/nrm3658 PMC Full Text View journal details
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