Conditional Disorder in Small Heat-shock Proteins.


Journal

Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R

Informations de publication

Date de publication:
17 04 2020
Historique:
received: 30 10 2019
revised: 27 01 2020
accepted: 09 02 2020
pubmed: 23 2 2020
medline: 31 10 2020
entrez: 22 2 2020
Statut: ppublish

Résumé

Small heat-shock proteins (sHSPs) are molecular chaperones that respond to cellular stresses to combat protein aggregation. HSP27 is a critical human sHSP that forms large, dynamic oligomers whose quaternary structures and chaperone activities depend on environmental factors. Upon exposure to cellular stresses, such as heat shock or acidosis, HSP27 oligomers can dissociate into dimers and monomers, which leads to significantly enhanced chaperone activity. The structured core of the protein, the α-crystallin domain (ACD), forms dimers and can prevent the aggregation of substrate proteins to a similar degree as the full-length protein. When the ACD dimer dissociates into monomers, it partially unfolds and exhibits enhanced activity. Here, we used solution-state NMR spectroscopy to characterize the structure and dynamics of the HSP27 ACD monomer. Web show that the monomer is stabilized at low pH and that its backbone chemical shifts,

Identifiants

pubmed: 32081587
pii: S0022-2836(20)30146-7
doi: 10.1016/j.jmb.2020.02.003
pmc: PMC7245567
mid: NIHMS1569786
pii:
doi:

Substances chimiques

HSPB1 protein, human 0
Heat-Shock Proteins 0
Molecular Chaperones 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

3033-3049

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/J018082/1
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : P41 GM111135
Pays : United States
Organisme : Intramural NIH HHS
ID : Z01 DK029046
Pays : United States
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/J014346/1
Pays : United Kingdom
Organisme : Intramural NIH HHS
ID : Z01 DK029048
Pays : United States

Informations de copyright

Copyright © 2020 Elsevier Ltd. All rights reserved.

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Auteurs

T Reid Alderson (TR)

Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.

Jinfa Ying (J)

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.

Ad Bax (A)

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA. Electronic address: bax@nih.gov.

Justin L P Benesch (JLP)

Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK. Electronic address: justin.benesch@chem.ox.ac.uk.

Andrew J Baldwin (AJ)

Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK. Electronic address: andrew.baldwin@chem.ox.ac.uk.

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Classifications MeSH