Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism

During stress conditions bacterial ribosomes dimerize and form inactive but stable hibernating 100S particles, a process that is facilitated by the hibernation-promoting factor (HPF). Here the authors analyze 100S dimer formation as a function of HPF protein concentration and present the Thermus the...

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Autores principales:	Rasmus Kock Flygaard, Niels Boegholm, Marat Yusupov, Lasse B. Jenner
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5cc48ee25d5f4ef09112efa40bc3bd60
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spelling	oai:doaj.org-article:5cc48ee25d5f4ef09112efa40bc3bd602021-12-02T16:56:53ZCryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism10.1038/s41467-018-06724-x2041-1723https://doaj.org/article/5cc48ee25d5f4ef09112efa40bc3bd602018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06724-xhttps://doaj.org/toc/2041-1723During stress conditions bacterial ribosomes dimerize and form inactive but stable hibernating 100S particles, a process that is facilitated by the hibernation-promoting factor (HPF). Here the authors analyze 100S dimer formation as a function of HPF protein concentration and present the Thermus thermophilus 100S ribosome cryo-EM structure.Rasmus Kock FlygaardNiels BoegholmMarat YusupovLasse B. JennerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Rasmus Kock Flygaard Niels Boegholm Marat Yusupov Lasse B. Jenner Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
description	During stress conditions bacterial ribosomes dimerize and form inactive but stable hibernating 100S particles, a process that is facilitated by the hibernation-promoting factor (HPF). Here the authors analyze 100S dimer formation as a function of HPF protein concentration and present the Thermus thermophilus 100S ribosome cryo-EM structure.
format	article
author	Rasmus Kock Flygaard Niels Boegholm Marat Yusupov Lasse B. Jenner
author_facet	Rasmus Kock Flygaard Niels Boegholm Marat Yusupov Lasse B. Jenner
author_sort	Rasmus Kock Flygaard
title	Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
title_short	Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
title_full	Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
title_fullStr	Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
title_full_unstemmed	Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
title_sort	cryo-em structure of the hibernating thermus thermophilus 100s ribosome reveals a protein-mediated dimerization mechanism
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/5cc48ee25d5f4ef09112efa40bc3bd60
work_keys_str_mv	AT rasmuskockflygaard cryoemstructureofthehibernatingthermusthermophilus100sribosomerevealsaproteinmediateddimerizationmechanism AT nielsboegholm cryoemstructureofthehibernatingthermusthermophilus100sribosomerevealsaproteinmediateddimerizationmechanism AT maratyusupov cryoemstructureofthehibernatingthermusthermophilus100sribosomerevealsaproteinmediateddimerizationmechanism AT lassebjenner cryoemstructureofthehibernatingthermusthermophilus100sribosomerevealsaproteinmediateddimerizationmechanism
_version_	1718382682385154048

Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism

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