Local unfolding of the HSP27 monomer regulates chaperone activity

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 substantial...

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Autores principales:	T. Reid Alderson, Julien Roche, Heidi Y. Gastall, David M. Dias, Iva Pritišanac, Jinfa Ying, Ad Bax, Justin L. P. Benesch, Andrew J. Baldwin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/550a85efe9614ed0b28d5ac8d6498385
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spelling	oai:doaj.org-article:550a85efe9614ed0b28d5ac8d64983852021-12-02T14:35:30ZLocal unfolding of the HSP27 monomer regulates chaperone activity10.1038/s41467-019-08557-82041-1723https://doaj.org/article/550a85efe9614ed0b28d5ac8d64983852019-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08557-8https://doaj.org/toc/2041-1723The 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.T. Reid AldersonJulien RocheHeidi Y. GastallDavid M. DiasIva PritišanacJinfa YingAd BaxJustin L. P. BeneschAndrew J. BaldwinNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q T. Reid Alderson Julien Roche Heidi Y. Gastall David M. Dias Iva Pritišanac Jinfa Ying Ad Bax Justin L. P. Benesch Andrew J. Baldwin Local unfolding of the HSP27 monomer regulates chaperone activity
description	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.
format	article
author	T. Reid Alderson Julien Roche Heidi Y. Gastall David M. Dias Iva Pritišanac Jinfa Ying Ad Bax Justin L. P. Benesch Andrew J. Baldwin
author_facet	T. Reid Alderson Julien Roche Heidi Y. Gastall David M. Dias Iva Pritišanac Jinfa Ying Ad Bax Justin L. P. Benesch Andrew J. Baldwin
author_sort	T. Reid Alderson
title	Local unfolding of the HSP27 monomer regulates chaperone activity
title_short	Local unfolding of the HSP27 monomer regulates chaperone activity
title_full	Local unfolding of the HSP27 monomer regulates chaperone activity
title_fullStr	Local unfolding of the HSP27 monomer regulates chaperone activity
title_full_unstemmed	Local unfolding of the HSP27 monomer regulates chaperone activity
title_sort	local unfolding of the hsp27 monomer regulates chaperone activity
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/550a85efe9614ed0b28d5ac8d6498385
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Local unfolding of the HSP27 monomer regulates chaperone activity

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