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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Main Authors: Gabriel Demo, Howard B. Gamper, Anna B. Loveland, Isao Masuda, Christine E. Carbone, Egor Svidritskiy, Ya-Ming Hou, Andrei A. Korostelev
Format: Article
Language:English
Published: Nature Publishing Group 2021-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-24911-1
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spelling doaj-9e96fbbefbf946cca2e64e5aa10017b32021-08-01T11:38:30ZengNature Publishing GroupNature Communications2041-17232021-07-0112111210.1038/s41467-021-24911-1Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocationGabriel Demo0Howard B. Gamper1Anna B. Loveland2Isao Masuda3Christine E. Carbone4Egor Svidritskiy5Ya-Ming Hou6Andrei A. Korostelev7RNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolDepartment of Biochemistry and Molecular Biology, Thomas Jefferson UniversityRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolDepartment of Biochemistry and Molecular Biology, Thomas Jefferson UniversityRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolDepartment of Biochemistry and Molecular Biology, Thomas Jefferson UniversityRNA Therapeutics Institute, Department of Biochemistry and Molecular Pharmacology, UMass Medical SchoolTranslational 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.https://doi.org/10.1038/s41467-021-24911-1
collection DOAJ
language English
format Article
sources DOAJ
author Gabriel Demo
Howard B. Gamper
Anna B. Loveland
Isao Masuda
Christine E. Carbone
Egor Svidritskiy
Ya-Ming Hou
Andrei A. Korostelev
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-07-01
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.
url https://doi.org/10.1038/s41467-021-24911-1
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