Evidence map›Paper›PMID 18538658›Full record

ArticleMolecular cell2008

Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination.

Hua Fan-Minogue, Ming Du, Andrey V Pisarev, Adam K Kallmeyer, Joe Salas-Marco, Kim M Keeling, Sunnie R Thompson, Tatyana V Pestova, David M Bedwell

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. 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
3.3field-weighted citation impact, top 8% 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, 67 citations in OpenAlex.

  1. RNAViruses · 2026
    Review
  2. Article
  3. Review
  4. Translation Phases in Eukaryotes.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Therapeutics based on stop codon readthrough.Annual review of genomics and human genetics · 2014
    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

9 authors at 2 institutions in 1 country.

Hua Fan-MinogueDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Ming Du
Andrey V Pisarev
Adam K Kallmeyer
Joe Salas-Marco
Kim M Keeling
Sunnie R Thompson
Tatyana V Pestova
David M Bedwell
University of Alabama at Birmingham · USSUNY Downstate Health Sciences University · US

Funding

THE MECHANISMS OF EUKARYOTIC TRANSLATION TERMINATION AND RIBOSOMAL RECYCLINGR01GM080623 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI PESTOVA, TATYANA V · 2007 to 2015
$2.7M
Mechanism of Eukaryotic Translation TerminationR01GM068854 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BEDWELL, DAVID M. · 2003 to 2011
$2.5M
NIGMS NIH HHS R01 GM068854NIGMS NIH HHS R01 GM080623NIGMS NIH HHS R01 GM 68854NIGMS NIH HHS R01 GM 80623
6 · The paper itself

Abstract

Organisms that use the standard genetic code recognize UAA, UAG, and UGA as stop codons, whereas variant code species frequently alter this pattern of stop codon recognition. We previously demonstrated that a hybrid eRF1 carrying the Euplotes octocarinatus domain 1 fused to Saccharomyces cerevisiae domains 2 and 3 (Eo/Sc eRF1) recognized UAA and UAG, but not UGA, as stop codons. In the current study, we identified mutations in Eo/Sc eRF1 that restore UGA recognition and define distinct roles for the TASNIKS and YxCxxxF motifs in eRF1 function. Mutations in or near the YxCxxxF motif support the cavity model for stop codon recognition by eRF1. Mutations in the TASNIKS motif eliminated the eRF3 requirement for peptide release at UAA and UAG codons, but not UGA codons. These results suggest that the TASNIKS motif and eRF3 function together to trigger eRF1 conformational changes that couple stop codon recognition and peptide release during eukaryotic translation termination.

Indexed as

Peptide Chain Termination, TranslationalAmino Acid MotifsAnimalsCodon, TerminatorEuplotesModels, BiologicalPeptidesPeptide Termination FactorsProtein ConformationRecombinant Fusion ProteinsSaccharomyces cerevisiaeSuppression, GeneticCodon, TerminatorPeptidesPeptide Termination FactorsRecombinant Fusion Proteins

Identifiers

PMID18538658
PMCPMC2475577
OpenAlexW2043870765

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.