Document Type
Article
Publication Date
7-30-2021
Abstract
Frameshifting of mRNA during translation provides a strategy to expand the coding repertoire of cells and viruses. How and where in the elongation cycle +1-frameshifting occurs remains poorly understood. We describe seven ~3.5-Å-resolution cryo-EM structures of 70S ribosome complexes, allowing visualization of elongation and translocation by the GTPase elongation factor G (EF-G). Four structures with a + 1-frameshifting-prone mRNA reveal that frameshifting takes place during translocation of tRNA and mRNA. Prior to EF-G binding, the pre-translocation complex features an in-frame tRNA-mRNA pairing in the A site. In the partially translocated structure with EF-G•GDPCP, the tRNA shifts to the +1-frame near the P site, rendering the freed mRNA base to bulge between the P and E sites and to stack on the 16S rRNA nucleotide G926. The ribosome remains frameshifted in the nearly post-translocation state. Our findings demonstrate that the ribosome and EF-G cooperate to induce +1 frameshifting during tRNA-mRNA translocation.
Recommended Citation
Demo, Gabriel; Gamper, Howard; Loveland, Anna B.; Masuda, Isao; Carbone, Christine E.; Svidritskiy, Egor; Hou, Ya-Ming; and Korostelev, Andrei A., "Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation." (2021). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 189.
https://jdc.jefferson.edu/bmpfp/189
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
PubMed ID
34330903
Language
English
Comments
This article is the authors’ final published version in Nature Communications, Volume 12, Issue 1, July 2021, Article number 4644.
The published version is available at https://doi.org/10.1038/s41467-021-24911-1. Copyright © Demo et al.