| DEMO, Gabriel, H.B. GAMPER, A.B. LOVELAND, I. MASUDA, C.E. CARBONE, E. SVIDRITSKIY, Y.M. HOU a A.A. KOROSTELEV. Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation. Nature Communications. London: Nature Publishing Group, 2021, roč. 12, č. 1, s. 4644-4655. ISSN 2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-021-24911-1. |
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@article{1836382,
author = {Demo, Gabriel and Gamper, H.B. and Loveland, A.B. and Masuda, I. and Carbone, C.E. and Svidritskiy, E. and Hou, Y.M. and Korostelev, A.A.},
article_location = {London},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41467-021-24911-1},
keywords = {RELEASE FACTOR-IITRANSFER-RNAANTICODON LOOPMESSENGER-RNAGENE-EXPRESSIONDECODING CENTERSUPPRESSORTRANSLATIONVISUALIZATIONMECHANISM},
language = {eng},
issn = {2041-1723},
journal = {Nature Communications},
title = {Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation},
url = {https://www.nature.com/articles/s41467-021-24911-1},
volume = {12},
year = {2021}
}
TY - JOUR
ID - 1836382
AU - Demo, Gabriel - Gamper, H.B. - Loveland, A.B. - Masuda, I. - Carbone, C.E. - Svidritskiy, E. - Hou, Y.M. - Korostelev, A.A.
PY - 2021
TI - Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation
JF - Nature Communications
VL - 12
IS - 1
SP - 4644
EP - 4644
PB - Nature Publishing Group
SN - 20411723
KW - RELEASE FACTOR-IITRANSFER-RNAANTICODON LOOPMESSENGER-RNAGENE-EXPRESSIONDECODING CENTERSUPPRESSORTRANSLATIONVISUALIZATIONMECHANISM
UR - https://www.nature.com/articles/s41467-021-24911-1
N2 - 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.
ER -
DEMO, Gabriel, H.B. GAMPER, A.B. LOVELAND, I. MASUDA, C.E. CARBONE, E. SVIDRITSKIY, Y.M. HOU a A.A. KOROSTELEV. Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation. \textit{Nature Communications}. London: Nature Publishing Group, 2021, roč.~12, č.~1, s.~4644-4655. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-021-24911-1.
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