GroEL actively stimulates folding of the endogenous substrate protein PepQ

In the prevailing model for assisted protein folding, chaperonins act passively by preventing protein aggregation. Here, the authors use single-molecule fluorescence measurements and cryo-electron microscopy and show that theE. coliGroELS chaperonin system also has an active role in folding the endo...

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Autores principales:	Jeremy Weaver, Mengqiu Jiang, Andrew Roth, Jason Puchalla, Junjie Zhang, Hays S. Rye
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0541f983daa94abab6070f16ff2a5940
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spelling	oai:doaj.org-article:0541f983daa94abab6070f16ff2a59402021-12-02T15:38:31ZGroEL actively stimulates folding of the endogenous substrate protein PepQ10.1038/ncomms159342041-1723https://doaj.org/article/0541f983daa94abab6070f16ff2a59402017-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms15934https://doaj.org/toc/2041-1723In the prevailing model for assisted protein folding, chaperonins act passively by preventing protein aggregation. Here, the authors use single-molecule fluorescence measurements and cryo-electron microscopy and show that theE. coliGroELS chaperonin system also has an active role in folding the endogenous bacterial protein PepQ.Jeremy WeaverMengqiu JiangAndrew RothJason PuchallaJunjie ZhangHays S. RyeNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jeremy Weaver Mengqiu Jiang Andrew Roth Jason Puchalla Junjie Zhang Hays S. Rye GroEL actively stimulates folding of the endogenous substrate protein PepQ
description	In the prevailing model for assisted protein folding, chaperonins act passively by preventing protein aggregation. Here, the authors use single-molecule fluorescence measurements and cryo-electron microscopy and show that theE. coliGroELS chaperonin system also has an active role in folding the endogenous bacterial protein PepQ.
format	article
author	Jeremy Weaver Mengqiu Jiang Andrew Roth Jason Puchalla Junjie Zhang Hays S. Rye
author_facet	Jeremy Weaver Mengqiu Jiang Andrew Roth Jason Puchalla Junjie Zhang Hays S. Rye
author_sort	Jeremy Weaver
title	GroEL actively stimulates folding of the endogenous substrate protein PepQ
title_short	GroEL actively stimulates folding of the endogenous substrate protein PepQ
title_full	GroEL actively stimulates folding of the endogenous substrate protein PepQ
title_fullStr	GroEL actively stimulates folding of the endogenous substrate protein PepQ
title_full_unstemmed	GroEL actively stimulates folding of the endogenous substrate protein PepQ
title_sort	groel actively stimulates folding of the endogenous substrate protein pepq
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/0541f983daa94abab6070f16ff2a5940
work_keys_str_mv	AT jeremyweaver groelactivelystimulatesfoldingoftheendogenoussubstrateproteinpepq AT mengqiujiang groelactivelystimulatesfoldingoftheendogenoussubstrateproteinpepq AT andrewroth groelactivelystimulatesfoldingoftheendogenoussubstrateproteinpepq AT jasonpuchalla groelactivelystimulatesfoldingoftheendogenoussubstrateproteinpepq AT junjiezhang groelactivelystimulatesfoldingoftheendogenoussubstrateproteinpepq AT hayssrye groelactivelystimulatesfoldingoftheendogenoussubstrateproteinpepq
_version_	1718386152538374144

GroEL actively stimulates folding of the endogenous substrate protein PepQ

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