Evidence map›Paper›PMID 26072700›Full record

ArticleNature communications2015

Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome.

Sarah Adio, Tamara Senyushkina, Frank Peske, Niels Fischer, Wolfgang Wintermeyer, Marina V Rodnina

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Recoding by NNature communications · 2026
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  2. RNAViruses · 2026
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  4. Modulation of translational decoding by mNature communications · 2023
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  7. Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  11. Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. New Insights into Ribosome Structure and Function.Cold Spring Harbor perspectives in biology · 2019
    Review
  17. Article
  18. The 2018 correlative microscopy techniques roadmap.Journal of physics D: Applied physics · 2018
    Review
  19. Article
  20. Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
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

6 authors.

Sarah AdioDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Goettingen 37077, Germany.
Tamara SenyushkinaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Goettingen 37077, Germany.
Frank PeskeDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Goettingen 37077, Germany.
Niels Fischer3D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, Goettingen 37077, Germany.
Wolfgang WintermeyerDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Goettingen 37077, Germany.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Goettingen 37077, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The coupled translocation of transfer RNA and messenger RNA through the ribosome entails large-scale structural rearrangements, including step-wise movements of the tRNAs. Recent structural work has visualized intermediates of translocation induced by elongation factor G (EF-G) with tRNAs trapped in chimeric states with respect to 30S and 50S ribosomal subunits. The functional role of the chimeric states is not known. Here we follow the formation of translocation intermediates by single-molecule fluorescence resonance energy transfer. Using EF-G mutants, a non-hydrolysable GTP analogue, and fusidic acid, we interfere with either translocation or EF-G release from the ribosome and identify several rapidly interconverting chimeric tRNA states on the reaction pathway. EF-G engagement prevents backward transitions early in translocation and increases the fraction of ribosomes that rapidly fluctuate between hybrid, chimeric and posttranslocation states. Thus, the engagement of EF-G alters the energetics of translocation towards a flat energy landscape, thereby promoting forward tRNA movement.

Indexed as

Crystallography, X-RayEscherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferPeptide Elongation Factor GProtein BiosynthesisRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialRNA, MessengerRNA, TransferEscherichia coli ProteinsPeptide Elongation Factor GRibosomal ProteinsRNA, MessengerRNA, TransferrplK protein, E coli

Identifiers

PMID26072700
PMCPMC4490557

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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.