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

G. Demo, HB. Gamper, AB. Loveland, I. Masuda, CE. Carbone, E. Svidritskiy, YM. Hou, AA. Korostelev

. 2021 ; 12 (1) : 4644. [pub] 20210730

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc21025287

Grantová podpora
R01 AI139202 NIAID NIH HHS - United States
R35 GM127094 NIGMS NIH HHS - United States
R35 GM134931 NIGMS NIH HHS - United States

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.

Citace poskytuje Crossref.org

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