A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy

When bacteria enter the stationary growth phase, protein translation is suppressed via the dimerization of 70S ribosomes into inactive complexes. Here the authors provide a structural basis for how the dual domain hibernation promotion factor promotes ribosome dimerization and hibernation in bacteri...

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Autores principales:	Linda E. Franken, Gert T. Oostergetel, Tjaard Pijning, Pranav Puri, Valentina Arkhipova, Egbert J. Boekema, Bert Poolman, Albert Guskov
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/399c1c026c834306bf7b09a8915fb0a1
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id	oai:doaj.org-article:399c1c026c834306bf7b09a8915fb0a1
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spelling	oai:doaj.org-article:399c1c026c834306bf7b09a8915fb0a12021-12-02T14:42:41ZA general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy10.1038/s41467-017-00718-x2041-1723https://doaj.org/article/399c1c026c834306bf7b09a8915fb0a12017-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00718-xhttps://doaj.org/toc/2041-1723When bacteria enter the stationary growth phase, protein translation is suppressed via the dimerization of 70S ribosomes into inactive complexes. Here the authors provide a structural basis for how the dual domain hibernation promotion factor promotes ribosome dimerization and hibernation in bacteria.Linda E. FrankenGert T. OostergetelTjaard PijningPranav PuriValentina ArkhipovaEgbert J. BoekemaBert PoolmanAlbert GuskovNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Linda E. Franken Gert T. Oostergetel Tjaard Pijning Pranav Puri Valentina Arkhipova Egbert J. Boekema Bert Poolman Albert Guskov A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy
description	When bacteria enter the stationary growth phase, protein translation is suppressed via the dimerization of 70S ribosomes into inactive complexes. Here the authors provide a structural basis for how the dual domain hibernation promotion factor promotes ribosome dimerization and hibernation in bacteria.
format	article
author	Linda E. Franken Gert T. Oostergetel Tjaard Pijning Pranav Puri Valentina Arkhipova Egbert J. Boekema Bert Poolman Albert Guskov
author_facet	Linda E. Franken Gert T. Oostergetel Tjaard Pijning Pranav Puri Valentina Arkhipova Egbert J. Boekema Bert Poolman Albert Guskov
author_sort	Linda E. Franken
title	A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy
title_short	A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy
title_full	A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy
title_fullStr	A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy
title_full_unstemmed	A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy
title_sort	general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/399c1c026c834306bf7b09a8915fb0a1
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A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy

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