Evidence map›Paper›PMID 22000017›Full record

ArticleCell2011

A primary role for release factor 3 in quality control during translation elongation in Escherichia coli.

Hani S Zaher, Rachel Green

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

42 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. A data-driven estimation of the ribosome drop-off rate inNAR genomics and bioinformatics · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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
  14. Article
  15. Article
  16. Article
  17. Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021
    Review
  18. Article
  19. Review
  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

2 authors at 2 institutions in 1 country.

Hani S ZaherHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Rachel Green
Howard Hughes Medical Institute · USJohns Hopkins University · 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
The molecular mechanism of post-peptidyl quality control on the ribosomeK99GM094210 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ZAHER, HANI · 2010 to 2011
$152k
Howard Hughes Medical InstituteNIGMS NIH HHS K99 GM094210NIGMS NIH HHS R00 GM094210NIGMS NIH HHS R01 GM059425
6 · The paper itself

Abstract

Release factor 3 (RF3) is a GTPase found in a broad range of bacteria where it is thought to play a critical "recycling" role in translation by facilitating the removal of class 1 release factors (RF1 and RF2) from the ribosome following peptide release. More recently, RF3 was shown in vitro to stimulate a retrospective editing reaction on the bacterial ribosome wherein peptides carrying mistakes are prematurely terminated during protein synthesis. Here, we examine the role of RF3 in the bacterial cell and show that the deletion of this gene sensitizes cells to other perturbations that reduce the overall fidelity of protein synthesis. We further document substantial effects on mRNA stability and protein expression using reporter systems, native mRNAs and proteins. We conclude that RF3 plays a primary role in vivo in specifying the fidelity of protein synthesis thus impacting overall protein quantity and quality.

Indexed as

Peptide Chain Elongation, TranslationalEscherichia coliEscherichia coli ProteinsFrameshifting, RibosomalMass SpectrometryPeptide Termination FactorsProtein BiosynthesisRNA StabilityEscherichia coli ProteinsPeptide Termination FactorsprfB protein, E coliprfC protein, E coli

Identifiers

PMID22000017
PMCPMC3415990
OpenAlexW2079262040

What OpenQuestion holds

Textmetadata
LicenceTDM
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.