Evidence map›Paper›PMID 19324963›Full record

ArticleRNA (New York, N.Y.)2009

Distinct functions of elongation factor G in ribosome recycling and translocation.

Andreas Savelsbergh, Marina V Rodnina, Wolfgang Wintermeyer

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
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

73 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. Mechanisms of fusidic acid resistance.Biochemical Society transactions · 2025
    Review
  3. Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. The role of GTP hydrolysis by EF-G in ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021
    Review
  15. Review
  16. Global reprogramming of virulence and antibiotic resistance inThe Journal of biological chemistry · 2020
    Article
  17. Article
  18. Contact Effect of aAntibiotics (Basel, Switzerland) · 2020
    Article
  19. Article
  20. Structural basis for ribosome recycling by RRF and tRNA.Nature structural & molecular biology · 2020
    Article

13 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Andreas SavelsberghInstitute of Molecular Biology, University of Witten/Herdecke, 58448 Witten, Germany.
Marina V Rodnina
Wolfgang Wintermeyer
Max Planck Society · DEWitten/Herdecke University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elongation factor G (EF-G) promotes the translocation step in bacterial protein synthesis and, together with ribosome recycling factor (RRF), the disassembly of the post-termination ribosome. Unlike translocation, ribosome disassembly strictly requires GTP hydrolysis by EF-G. Here we report that ribosome disassembly is strongly inhibited by vanadate, an analog of inorganic phosphate (Pi), indicating that Pi release is required for ribosome disassembly. In contrast, the function of EF-G in single-round translocation is not affected by vanadate, while the turnover reaction is strongly inhibited. We also show that the antibiotic fusidic acid blocks ribosome disassembly by EF-G/RRF at a 1000-fold lower concentration than required for the inhibition of EF-G turnover in vitro and close to the effective inhibitory concentration in vivo, suggesting that the antimicrobial activity of fusidic acid is primarily due to the direct inhibition of ribosome recycling. Our results indicate that conformational coupling between EF-G and the ribosome is principally different in translocation and ribosome disassembly. Pi release is not required for the mechanochemical function of EF-G in translocation, whereas the interactions between RRF and EF-G introduce tight coupling between the conformational change of EF-G induced by Pi release and ribosome disassembly.

Indexed as

BacteriaFusidic AcidGuanosine TriphosphatePeptide Elongation Factor GPhosphatesRibosomal ProteinsRibosomesFusidic AcidGuanosine TriphosphatePeptide Elongation Factor GPhosphatesRibosomal Proteinsribosome releasing factor

Identifiers

PMID19324963
PMCPMC2673078
OpenAlexW2102724075

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.