Evidence map›Paper›PMID 33555093›Full record

ArticleThe EMBO journal2021

Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation.

Namit Ranjan, Agnieszka A Pochopien, Colin Chih-Chien Wu, Bertrand Beckert, Sandra Blanchet, Rachel Green, Marina V Rodnina, Daniel N Wilson

Abstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Structure of a Gcn2 dimer in complex with the large 60S ribosomal subunit.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Capturing eukaryotic ribosome dynamics in situ at high resolution.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. RiboScreenInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. The geneFrontiers in microbiology · 2024
    Article
  14. Article
  15. Article
  16. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Namit RanjanDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-6032-0319
Agnieszka A PochopienGene Center, Department for Biochemistry and Center for integrated Protein Science Munich (CiPSM), University of Munich, Munich, Germany.
Colin Chih-Chien WuDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Bertrand BeckertInstitute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany.
Sandra BlanchetDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Rachel GreenDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0001-9337-2003
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-0105-3879
Daniel N WilsonGene Center, Department for Biochemistry and Center for integrated Protein Science Munich (CiPSM), University of Munich, Munich, Germany.ORCID 0000-0003-3816-3828

Funding

Molecular mechanisms of ribosome pausing and the cellular responseR37GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2014 to 2023
$3.5M
Howard Hughes Medical InstituteNIGMS NIH HHS R37 GM059425
6 · The paper itself

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 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.

Indexed as

Cryoelectron MicroscopyPeptide Elongation FactorsProtein BiosynthesisRibosomesRNA, MessengerRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranslocation, GeneticPeptide Elongation FactorsRNA, MessengerRNA, TransferSaccharomyces cerevisiae ProteinsYEF3 protein, S cerevisiaeABC ATPasecryo-EMeEF3E-site tRNAL1 stalk

Identifiers

PMID33555093
PMCPMC7957392

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.