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

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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:	Simultaneous gene transcription and translation