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It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate

Abstract:

Small heat-shock proteins (sHsps) are ubiquitous molecular chaperones, and sHsp mutations or altered expression are linked to multiple human disease states. sHsp monomers assemble into large oligomers with dimeric substructure, and the dynamics of sHsp oligomers has led to major questions about the form that captures substrate, a critical aspect of their mechanism of action. We show here that sub-structural dimers of two plant dodecameric sHsps, Ta16.9 and homologous Ps18.1, are functional un...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1074/jbc.ra118.005421

Authors


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Role:
Author
ORCID:
0000-0002-3039-8123
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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Oxford college:
University College
Role:
Author
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Name:
Engineering and Physical Sciences Research Council
Funding agency for:
Vierling, E
Grant:
EP/J01835X/1
EP/P016499/1
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Name:
National Institutes of Health
Grant:
RO1 GM42762
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Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/K004247/1
Publisher:
American Society for Biochemistry and Molecular Biology
Journal:
Journal of Biological Chemistry More from this journal
Volume:
293
Issue:
51
Pages:
19511-19521
Publication date:
2018-10-22
Acceptance date:
2018-10-22
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pmid:
30348902
Language:
English
Keywords:
Pubs id:
pubs:935174
UUID:
uuid:4beaec0a-ac32-4cb5-9ace-cef569cbeaed
Local pid:
pubs:935174
Source identifiers:
935174
Deposit date:
2018-11-29

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