Local unfolding of the HSP27 monomer regulates chaperone activity

T. Reid Alderson; Julien Roche; Heidi Y. Gastall; David M. Dias; Iva Pritišanac; Jinfa Ying; Ad Bax; Justin L. P. Benesch; Andrew J. Baldwin

doi:10.1038/s41467-019-08557-8

Nature Communications (Mar 2019)

Local unfolding of the HSP27 monomer regulates chaperone activity

T. Reid Alderson,
Julien Roche,
Heidi Y. Gastall,
David M. Dias,
Iva Pritišanac,
Jinfa Ying,
Ad Bax,
Justin L. P. Benesch,
Andrew J. Baldwin

Affiliations

T. Reid Alderson: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
Julien Roche: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Heidi Y. Gastall: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
David M. Dias: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
Iva Pritišanac: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
Jinfa Ying: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Ad Bax: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Justin L. P. Benesch: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
Andrew J. Baldwin: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford

DOI: https://doi.org/10.1038/s41467-019-08557-8
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 16

Abstract

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The small heat-shock protein HSP27 occurs predominantly in oligomeric forms, which makes its structural characterisation challenging. Here the authors employ CPMG and high-pressure NMR with native mass spectrometry and biophysical assays to show that the active monomeric form of HSP27 is substantially disordered and highly chaperone-active.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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