Evidence map›Paper›PMID 24667215›Full record

ArticleRNA (New York, N.Y.)2014

RF3:GTP promotes rapid dissociation of the class 1 termination factor.

Kristin S Koutmou, Megan E McDonald, Julie L Brunelle, Rachel Green

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 40 citations in OpenAlex.

  1. A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. At the Crossroad of Nucleotide Dynamics and Protein Synthesis in Bacteria.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Single-Molecule Fluorescence Applied to Translation.Cold Spring Harbor perspectives in biology · 2019
    Review
  13. Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  14. Article
  15. Article
  16. Review
  17. Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Article
  20. Ribosome pausing, arrest and rescue in bacteria and eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    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

4 authors at 1 institution in 1 country.

Kristin S Koutmou
Megan E McDonald
Julie L Brunelle
Rachel Green
Howard Hughes Medical Institute · US

Funding

Molecular mechanisms of ribosome pausing and the cellular responseR37GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2014 to 2023
$3.5M
The role played by the RNAs and tRNAs in translationR01GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1999 to 2013
$3.4M
Mechanism and targets of non-stop decay in eukaryotic translationF32GM100608 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KOUTMOU, KRISTIN S · 2012 to 2014
$169k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM100608NIGMS NIH HHS GM059425NIGMS NIH HHS R01 GM059425NIGMS NIH HHS R37 GM059425
6 · The paper itself

Abstract

Translation termination is promoted by class 1 and class 2 release factors in all domains of life. While the role of the bacterial class 1 factors, RF1 and RF2, in translation termination is well understood, the precise contribution of the bacterial class 2 release factor, RF3, to this process remains less clear. Here, we use a combination of binding assays and pre-steady state kinetics to provide a kinetic and thermodynamic framework for understanding the role of the translational GTPase RF3 in bacterial translation termination. First, we find that GDP and GTP have similar affinities for RF3 and that, on average, the t1/2 for nucleotide dissociation from the protein is 1-2 min. We further show that RF3:GDPNP, but not RF3:GDP, tightly associates with the ribosome pre- and post-termination complexes. Finally, we use stopped-flow fluorescence to demonstrate that RF3:GTP enhances RF1 dissociation rates by over 500-fold, providing the first direct observation of this step. Importantly, catalytically inactive variants of RF1 are not rapidly dissociated from the ribosome by RF3:GTP, arguing that a rotated state of the ribosome must be sampled for this step to efficiently occur. Together, these data define a more precise role for RF3 in translation termination and provide insights into the function of this family of translational GTPases.

Indexed as

Protein BiosynthesisCatalysisEscherichia coliEscherichia coli ProteinsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateKineticsNucleotidesPeptide Termination FactorsProtein BindingRibosomesThermodynamicsEscherichia coli ProteinsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateNucleotidesPeptide Termination FactorsprfC protein, E coliRF3ribosometranslational GTPasetranslation termination

Identifiers

PMID24667215
PMCPMC3988563
OpenAlexW2101730674

What OpenQuestion holds

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LicenceCC BY
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.