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

Warning

This publication doesn't include Faculty of Economics and Administration. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

DEMO Gabriel GAMPER H.B. LOVELAND A.B. MASUDA I. CARBONE C.E. SVIDRITSKIY E. HOU Y.M. KOROSTELEV A.A.

Year of publication 2021
Type Article in Periodical
Magazine / Source Nature Communications
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://www.nature.com/articles/s41467-021-24911-1
Doi http://dx.doi.org/10.1038/s41467-021-24911-1
Keywords RELEASE FACTOR-IITRANSFER-RNAANTICODON LOOPMESSENGER-RNAGENE-EXPRESSIONDECODING CENTERSUPPRESSORTRANSLATIONVISUALIZATIONMECHANISM
Description 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 similar to 3.5-angstrom-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 center dot 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.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.