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

Gabriel Demo, Howard B. Gamper, Anna B. Loveland, Isao Masuda, Christine E. Carbone, Egor Svidritskiy, Ya-Ming Hou () and Andrei A. Korostelev ()
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Gabriel Demo: UMass Medical School
Howard B. Gamper: Thomas Jefferson University
Anna B. Loveland: UMass Medical School
Isao Masuda: Thomas Jefferson University
Christine E. Carbone: UMass Medical School
Egor Svidritskiy: UMass Medical School
Ya-Ming Hou: Thomas Jefferson University
Andrei A. Korostelev: UMass Medical School

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-24911-1

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