The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy

Translation termination is under strong selection pressure for high speed and accuracy. Here the authors provide a 3D view of the dynamics of a translating bacterial ribosome as it recruits a class-1 release factor (RF1 or RF2) upon encountering a stop codon, and propose a structure-based kinetic mo...

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Autores principales:	Ziao Fu, Gabriele Indrisiunaite, Sandip Kaledhonkar, Binita Shah, Ming Sun, Bo Chen, Robert A. Grassucci, Måns Ehrenberg, Joachim Frank
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9745cb8c9f6c4f9bb405361ab774e80c
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spelling	oai:doaj.org-article:9745cb8c9f6c4f9bb405361ab774e80c2021-12-02T15:35:31ZThe structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy10.1038/s41467-019-10608-z2041-1723https://doaj.org/article/9745cb8c9f6c4f9bb405361ab774e80c2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10608-zhttps://doaj.org/toc/2041-1723Translation termination is under strong selection pressure for high speed and accuracy. Here the authors provide a 3D view of the dynamics of a translating bacterial ribosome as it recruits a class-1 release factor (RF1 or RF2) upon encountering a stop codon, and propose a structure-based kinetic model for the early steps in bacterial translation termination.Ziao FuGabriele IndrisiunaiteSandip KaledhonkarBinita ShahMing SunBo ChenRobert A. GrassucciMåns EhrenbergJoachim FrankNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ziao Fu Gabriele Indrisiunaite Sandip Kaledhonkar Binita Shah Ming Sun Bo Chen Robert A. Grassucci Måns Ehrenberg Joachim Frank The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
description	Translation termination is under strong selection pressure for high speed and accuracy. Here the authors provide a 3D view of the dynamics of a translating bacterial ribosome as it recruits a class-1 release factor (RF1 or RF2) upon encountering a stop codon, and propose a structure-based kinetic model for the early steps in bacterial translation termination.
format	article
author	Ziao Fu Gabriele Indrisiunaite Sandip Kaledhonkar Binita Shah Ming Sun Bo Chen Robert A. Grassucci Måns Ehrenberg Joachim Frank
author_facet	Ziao Fu Gabriele Indrisiunaite Sandip Kaledhonkar Binita Shah Ming Sun Bo Chen Robert A. Grassucci Måns Ehrenberg Joachim Frank
author_sort	Ziao Fu
title	The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
title_short	The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
title_full	The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
title_fullStr	The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
title_full_unstemmed	The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
title_sort	structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/9745cb8c9f6c4f9bb405361ab774e80c
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The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy

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