Evidence map›Paper›PMID 25636454›Full record

ArticleMolecular genetics and genomics : MGG2015

Interactions of release factor RF3 with the translation machinery.

Michael O'Connor

Abstract read
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In one paragraph

Article in Molecular genetics and genomics : MGG, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Single-Molecule Fluorescence Applied to Translation.Cold Spring Harbor perspectives in biology · 2019
    Review
  6. Pseudouridine-Free Escherichia coli Ribosomes.Journal of bacteriology · 2018
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. 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

1 author.

Michael O'ConnorSchool of Biological Sciences, University of Missouri-Kansas City, 5007 Rockhill Rd., Kansas City, MO, 64110, USA, oconnormi@umkc.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial release factor RF3 is a GTPase that has been implicated in multiple, incompletely understood steps of protein synthesis. This study explores the genetic interaction of RF3 with other components of the translation machinery. RF3 contributes to translation termination by recycling the class I release factors RF1 and RF2 off post-termination ribosomes. RF3 has also been implicated in dissociation of peptidyl-tRNAs from elongating ribosomes and in a post-peptidyltransferase quality control (post-PT QC) mechanism that selectively terminates ribosomes carrying erroneous peptides. A majority of the in vivo studies on RF3 have been carried out in K-12 strains of Escherichia coli which carry a partially defective RF2 protein with an Ala to Thr substitution at position 246. Here, the contribution of the K-12 specific RF2 variant to RF3 activities has been investigated. Strain reconstruction experiments in both E. coli and Salmonella enterica demonstrate that defects in termination and post-PT QC that are associated with RF3 loss, as well as phenotypes uncovered by phenotypic profiling, are all substantially ameliorated when the incompletely active K-12-specific RF2 protein is replaced by a fully active Ala246 RF2. These results indicate that RF3 loss is well tolerated in bacteria with fully active class I release factors, but that many of the previously reported phenotypes for RF3 deletion strains have been compromised by the presence of a partially defective RF2.

Indexed as

Protein BiosynthesisAnti-Bacterial AgentsBacterial ProteinsCefsulodinEscherichia coliEscherichia coli ProteinsMicrobial ViabilityMutationPeptide Chain Termination, TranslationalPeptide Termination FactorsPhenotypeProtein BindingRibosomesRNA, Transfer, Amino AcylSalmonella entericaAnti-Bacterial AgentsBacterial ProteinsCefsulodinEscherichia coli ProteinsPeptide Termination FactorsprfA protein, E coliprfB protein, E coliprfC protein, E coliRNA, Transfer, Amino AcyltRNA, peptidyl-

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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.