Evidence map›Paper›PMID 25735746›Full record

ArticleNucleic acids research2015

New insights into stop codon recognition by eRF1.

Sandra Blanchet, Michelle Rowe, Tobias Von der Haar, Céline Fabret, Stéphane Demais, Mark J Howard, Olivier Namy

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. RNAViruses · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Factors Affecting Readthrough of Natural Versus Premature Termination Codons.Advances in experimental medicine and biology · 2023
    Review
  10. Review
  11. Nonsense suppression therapies in human genetic diseases.Cellular and molecular life sciences : CMLS · 2021
    Review
  12. Review
  13. Dbp5/DDX19 between Translational Readthrough and Nonsense Mediated Decay.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  18. 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
  19. Article
  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

7 authors at 2 institutions in 2 countries.

Sandra BlanchetInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Batiment 400, 91400 Orsay, France.
Michelle RoweSchool of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Tobias Von der HaarSchool of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Céline FabretInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Batiment 400, 91400 Orsay, France.
Stéphane DemaisInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Batiment 400, 91400 Orsay, France.
Mark J HowardSchool of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Olivier NamyInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Batiment 400, 91400 Orsay, France olivier.namy@igmors.u-psud.fr.
Institut de Biologie Intégrative de la Cellule · FRUniversity of Kent · GB

Funding

Wellcome Trust 091163/Z/10/Z
6 · The paper itself

Abstract

In eukaryotes, translation termination is performed by eRF1, which recognizes stop codons via its N-terminal domain. Many previous studies based on point mutagenesis, cross-linking experiments or eRF1 chimeras have investigated the mechanism by which the stop signal is decoded by eRF1. Conserved motifs, such as GTS and YxCxxxF, were found to be important for termination efficiency, but the recognition mechanism remains unclear. We characterized a region of the eRF1 N-terminal domain, the P1 pocket, that we had previously shown to be involved in termination efficiency. We performed alanine scanning mutagenesis of this region, and we quantified in vivo readthrough efficiency for each alanine mutant. We identified two residues, arginine 65 and lysine 109, as critical for recognition of the three stop codons. We also demonstrated a role for the serine 33 and serine 70 residues in UGA decoding in vivo. NMR analysis of the alanine mutants revealed that the correct conformation of this region was controlled by the YxCxxxF motif. By combining our genetic data with a structural analysis of eRF1 mutants, we were able to formulate a new model in which the stop codon interacts with eRF1 through the P1 pocket.

Indexed as

Codon, TerminatorModels, MolecularMutagenesisNuclear Magnetic Resonance, BiomolecularPeptide Termination FactorsProtein ConformationProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiae ProteinsCodon, TerminatorETF1 protein, humanPeptide Termination FactorsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSUP45 protein, S cerevisiae

Identifiers

PMID25735746
PMCPMC4381064
OpenAlexW2162762051

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.