Evidence map›Paper›PMID 24798339›Full record

ArticleThe Journal of biological chemistry2014

Distinct roles for release factor 1 and release factor 2 in translational quality control.

Alexandros D Petropoulos, Megan E McDonald, Rachel Green, Hani S Zaher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  5. Article
  6. Article
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  8. Article
  9. Article
  10. Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021
    Review
  11. Article
  12. Review
  13. Article
  14. Decoding on the ribosome depends on the structure of the mRNA phosphodiester backbone.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 3 institutions in 1 country.

Alexandros D PetropoulosFrom the Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and.
Megan E McDonaldFrom the Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and.
Rachel GreenFrom the Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and.
Hani S Zaherthe Department of Biology, Washington University in St. Louis, St. Louis, Missouri 63130 hzaher@wustl.edu.
Howard Hughes Medical Institute · USJohns Hopkins University · USWashington University in St. Louis · US

Funding

The role played by the RNAs and tRNAs in translationR01GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1999 to 2013
$3.4M
The molecular mechanism of post-peptidyl quality control on the ribosomeR00GM094210 · NIGMS · WASHINGTON UNIVERSITY · PI ZAHER, HANI · 2012 to 2014
$728k
Howard Hughes Medical InstituteNIGMS NIH HHS R00 GM094210NIGMS NIH HHS R00GM094210NIGMS NIH HHS R01 GM059425NIGMS NIH HHS R01GM059425-06A1
6 · The paper itself

Abstract

In bacteria, stop codons are recognized by two similar class 1 release factors, release factor 1 (RF1) and release factor 2 (RF2). Normally, during termination, the class 2 release factor 3 (RF3), a GTPase, functions downstream of peptide release where it accelerates the dissociation of RF1/RF2 prior to ribosome recycling. In addition to their canonical function in termination, both classes of release factor are also involved in a post peptidyl transfer quality control (post PT QC) mechanism where the termination factors recognize mismatched (i.e. error-containing) ribosome complexes and promote premature termination. Here, using a well defined in vitro system, we explored the role of release factors in canonical termination and post PT QC. As reported previously, during canonical termination, RF1 and RF2 recognize stop codons in a similar manner, and RF3 accelerates their rate of dissociation. During post PT QC, only RF2 (and not RF1) effectively binds to mismatched ribosome complexes; and whereas the addition of RF3 to RF2 increased its rate of release on mismatched complexes, the addition of RF3 to RF1 inhibited its rate of release but increased the rate of peptidyl-tRNA dissociation. Our data strongly suggest that RF2, in addition to its primary role in peptide release, functions as the principle factor for post PT QC.

Indexed as

Escherichia coliEscherichia coli ProteinsPeptide Chain Termination, TranslationalPeptide Termination FactorsRibosomesEscherichia coli ProteinsPeptide Termination FactorsprfA protein, E coliprfB protein, E coliProtein SynthesisRibosomeTranslationTranslation ControlTranslation Release Factor

Identifiers

PMID24798339
PMCPMC4067194
OpenAlexW2019741974

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.