Evidence map›Paper›PMID 34413231›Full record

ArticleScience (New York, N.Y.)2021

Mechanisms that ensure speed and fidelity in eukaryotic translation termination.

Michael R Lawson, Laura N Lessen, Jinfan Wang, Arjun Prabhakar, Nicholas C Corsepius, Rachel Green, Joseph D Puglisi

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 65 citations in OpenAlex.

  1. Ribosome stalling position, spacing, and A-site occupancy impact translation and cotranslational mRNA decay in plants.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. RNAViruses · 2026
    Review
  3. Article
  4. Article
  5. RiboScreenBiomedicines · 2026
    Review
  6. Regulatory landscape of widespread stop codon readthrough inbioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024
    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 3 institutions in 1 country.

Michael R Lawson *Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0003-3554-8423
Laura N Lessen *Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0001-6155-3627
Jinfan WangDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID 0000-0003-4170-9289
Arjun PrabhakarDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-5589-2558
Nicholas C CorsepiusProgram in Molecular Biophysics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Rachel GreenDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA. ragreen@jhmi.edu puglisi@stanford.edu.ORCID 0000-0001-9337-2003
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA. ragreen@jhmi.edu puglisi@stanford.edu.ORCID 0000-0001-9268-5112
Stanford University · USHoward Hughes Medical Institute · USJohns Hopkins University · US

Funding

STRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7M
Molecular mechanisms of ribosome pausing and the cellular responseR37GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2014 to 2023
$3.5M
Dynamics of eukaryotic translation initiation and its controlR01GM113078 · NIGMS · STANFORD UNIVERSITY · PI PUGLISI, JOSEPH D · 2016 to 2021
$2.9M
NIGMS NIH HHS R01 GM051266NIGMS NIH HHS R01 GM113078NIGMS NIH HHS R37 GM059425
6 · The paper itself

Abstract

Translation termination, which liberates a nascent polypeptide from the ribosome specifically at stop codons, must occur accurately and rapidly. We established single-molecule fluorescence assays to track the dynamics of ribosomes and two requisite release factors (eRF1 and eRF3) throughout termination using an in vitro-reconstituted yeast translation system. We found that the two eukaryotic release factors bound together to recognize stop codons rapidly and elicit termination through a tightly regulated, multistep process that resembles transfer RNA selection during translation elongation. Because the release factors are conserved from yeast to humans, the molecular events that underlie yeast translation termination are likely broadly fundamental to eukaryotic protein synthesis.

Indexed as

Peptide Chain Termination, TranslationalCodon, TerminatorFluorescence Resonance Energy TransferPeptide Termination FactorsProtein BindingProtein BiosynthesisRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSingle Molecule ImagingCodon, Terminatorpeptide-chain-release factor 3Peptide Termination FactorsSaccharomyces cerevisiae ProteinsSUP45 protein, S cerevisiae

Identifiers

PMID34413231
PMCPMC9017434
OpenAlexW3193933253

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.