H2020 Marie Curie Actions of the European Commission
2643
Howard Hughes Medical Institute (HHMI)
German Research Foundation (DFG)
WI3285/8-1
Leibniz Association
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R37GM059425
Citation
Journal: EMBO J / Year: 2021 Title: Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation. Authors: Namit Ranjan / Agnieszka A Pochopien / Colin Chih-Chien Wu / Bertrand Beckert / Sandra Blanchet / Rachel Green / Marina V Rodnina / Daniel N Wilson / Abstract: In addition to the conserved translation elongation factors eEF1A and eEF2, fungi require a third essential elongation factor, eEF3. While eEF3 has been implicated in tRNA binding and release at the ...In addition to the conserved translation elongation factors eEF1A and eEF2, fungi require a third essential elongation factor, eEF3. While eEF3 has been implicated in tRNA binding and release at the ribosomal A and E sites, its exact mechanism of action is unclear. Here, we show that eEF3 acts at the mRNA-tRNA translocation step by promoting the dissociation of the tRNA from the E site, but independent of aminoacyl-tRNA recruitment to the A site. Depletion of eEF3 in vivo leads to a general slowdown in translation elongation due to accumulation of ribosomes with an occupied A site. Cryo-EM analysis of native eEF3-ribosome complexes shows that eEF3 facilitates late steps of translocation by favoring non-rotated ribosomal states, as well as by opening the L1 stalk to release the E-site tRNA. Additionally, our analysis provides structural insights into novel translation elongation states, enabling presentation of a revised yeast translation elongation cycle.
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Dec 9, 2020
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Mar 10, 2021
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Mar 10, 2021
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Jul 7, 2021
Processing site: PDBe / Status: Released
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