Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein

The Hsp70 system prevents protein aggregation and increases folding yields, but it is unknown whether it also enhances the rate of folding. Here the authors combine refolding assays, FRET and hydrogen/deuterium exchange-mass spectrometry measurements to study the folding of firefly luciferase and fi...

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Autores principales:	Rahmi Imamoglu, David Balchin, Manajit Hayer-Hartl, F. Ulrich Hartl
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6125957e2a10438cac86795beb9c3d88
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spelling	oai:doaj.org-article:6125957e2a10438cac86795beb9c3d882021-12-02T14:40:43ZBacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein10.1038/s41467-019-14245-42041-1723https://doaj.org/article/6125957e2a10438cac86795beb9c3d882020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-14245-4https://doaj.org/toc/2041-1723The Hsp70 system prevents protein aggregation and increases folding yields, but it is unknown whether it also enhances the rate of folding. Here the authors combine refolding assays, FRET and hydrogen/deuterium exchange-mass spectrometry measurements to study the folding of firefly luciferase and find that the bacterial Hsp70 actively promotes the folding of this multi-domain protein.Rahmi ImamogluDavid BalchinManajit Hayer-HartlF. Ulrich HartlNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Rahmi Imamoglu David Balchin Manajit Hayer-Hartl F. Ulrich Hartl Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
description	The Hsp70 system prevents protein aggregation and increases folding yields, but it is unknown whether it also enhances the rate of folding. Here the authors combine refolding assays, FRET and hydrogen/deuterium exchange-mass spectrometry measurements to study the folding of firefly luciferase and find that the bacterial Hsp70 actively promotes the folding of this multi-domain protein.
format	article
author	Rahmi Imamoglu David Balchin Manajit Hayer-Hartl F. Ulrich Hartl
author_facet	Rahmi Imamoglu David Balchin Manajit Hayer-Hartl F. Ulrich Hartl
author_sort	Rahmi Imamoglu
title	Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
title_short	Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
title_full	Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
title_fullStr	Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
title_full_unstemmed	Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
title_sort	bacterial hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/6125957e2a10438cac86795beb9c3d88
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Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein

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