Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation

Translational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the ribosome and EF-G to induce +1 frameshifting during t...

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Autores principales:	Gabriel Demo, Howard B. Gamper, Anna B. Loveland, Isao Masuda, Christine E. Carbone, Egor Svidritskiy, Ya-Ming Hou, Andrei A. Korostelev
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9e96fbbefbf946cca2e64e5aa10017b3
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spelling	oai:doaj.org-article:9e96fbbefbf946cca2e64e5aa10017b32021-12-02T16:13:27ZStructural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation10.1038/s41467-021-24911-12041-1723https://doaj.org/article/9e96fbbefbf946cca2e64e5aa10017b32021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24911-1https://doaj.org/toc/2041-1723Translational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the ribosome and EF-G to induce +1 frameshifting during the translocation step.Gabriel DemoHoward B. GamperAnna B. LovelandIsao MasudaChristine E. CarboneEgor SvidritskiyYa-Ming HouAndrei A. KorostelevNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Gabriel Demo Howard B. Gamper Anna B. Loveland Isao Masuda Christine E. Carbone Egor Svidritskiy Ya-Ming Hou Andrei A. Korostelev Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
description	Translational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the ribosome and EF-G to induce +1 frameshifting during the translocation step.
format	article
author	Gabriel Demo Howard B. Gamper Anna B. Loveland Isao Masuda Christine E. Carbone Egor Svidritskiy Ya-Ming Hou Andrei A. Korostelev
author_facet	Gabriel Demo Howard B. Gamper Anna B. Loveland Isao Masuda Christine E. Carbone Egor Svidritskiy Ya-Ming Hou Andrei A. Korostelev
author_sort	Gabriel Demo
title	Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
title_short	Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
title_full	Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
title_fullStr	Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
title_full_unstemmed	Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
title_sort	structural basis for +1 ribosomal frameshifting during ef-g-catalyzed translocation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/9e96fbbefbf946cca2e64e5aa10017b3
work_keys_str_mv	AT gabrieldemo structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation AT howardbgamper structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation AT annabloveland structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation AT isaomasuda structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation AT christineecarbone structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation AT egorsvidritskiy structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation AT yaminghou structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation AT andreiakorostelev structuralbasisfor1ribosomalframeshiftingduringefgcatalyzedtranslocation
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Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation

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