Evidence map›Paper›PMID 30873535›Full record

ArticleNucleic acids research2019

Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3.

Christian Beißel, Bettina Neumann, Simon Uhse, Irene Hampe, Prajwal Karki, Heike Krebber

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. RNA mProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Translation ofBiomedicines · 2021
    Article
  14. Nonsense suppression therapies in human genetic diseases.Cellular and molecular life sciences : CMLS · 2021
    Review
  15. Review
  16. Review
  17. Article
  18. Dbp5/DDX19 between Translational Readthrough and Nonsense Mediated Decay.International journal of molecular sciences · 2020
    Review
  19. 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

6 authors at 2 institutions in 1 country.

Christian BeißelAbteilung für Molekulare Genetik, Institut für Mikrobiologie und Genetik, Göttinger Zentrum für Molekulare Biowissenschaften (GZMB), Georg-August Universität Göttingen, Germany.
Bettina NeumannAbteilung für Molekulare Genetik, Institut für Mikrobiologie und Genetik, Göttinger Zentrum für Molekulare Biowissenschaften (GZMB), Georg-August Universität Göttingen, Germany.
Simon UhseAbteilung für Molekulare Genetik, Institut für Mikrobiologie und Genetik, Göttinger Zentrum für Molekulare Biowissenschaften (GZMB), Georg-August Universität Göttingen, Germany.
Irene HampeAbteilung für Molekulare Genetik, Institut für Mikrobiologie und Genetik, Göttinger Zentrum für Molekulare Biowissenschaften (GZMB), Georg-August Universität Göttingen, Germany.
Prajwal KarkiDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Heike KrebberAbteilung für Molekulare Genetik, Institut für Mikrobiologie und Genetik, Göttinger Zentrum für Molekulare Biowissenschaften (GZMB), Georg-August Universität Göttingen, Germany.
University of Göttingen · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translation termination requires eRF1 and eRF3 for polypeptide- and tRNA-release on stop codons. Additionally, Dbp5/DDX19 and Rli1/ABCE1 are required; however, their function in this process is currently unknown. Using a combination of in vivo and in vitro experiments, we show that they regulate a stepwise assembly of the termination complex. Rli1 and eRF3-GDP associate with the ribosome first. Subsequently, Dbp5-ATP delivers eRF1 to the stop codon and in this way prevents a premature access of eRF3. Dbp5 dissociates upon placing eRF1 through ATP-hydrolysis. This in turn enables eRF1 to contact eRF3, as the binding of Dbp5 and eRF3 to eRF1 is mutually exclusive. Defects in the Dbp5-guided eRF1 delivery lead to premature contact and premature dissociation of eRF1 and eRF3 from the ribosome and to subsequent stop codon readthrough. Thus, the stepwise Dbp5-controlled termination complex assembly is essential for regular translation termination events. Our data furthermore suggest a possible role of Dbp5/DDX19 in alternative translation termination events, such as during stress response or in developmental processes, which classifies the helicase as a potential drug target for nonsense suppression therapy to treat cancer and neurodegenerative diseases.

Indexed as

Peptide Chain Termination, TranslationalCodon, TerminatorDEAD-box RNA HelicasesGuanosine TriphosphateNucleocytoplasmic Transport ProteinsPeptide Termination FactorsProtein BindingProtein BiosynthesisRibosomesRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCodon, TerminatorDBP5 protein, S cerevisiaeDEAD-box RNA HelicasesGuanosine TriphosphateNucleocytoplasmic Transport Proteinspeptide-chain-release factor 3Peptide Termination FactorsRNA, TransferSaccharomyces cerevisiae ProteinsSUP45 protein, S cerevisiae

Identifiers

PMID30873535
PMCPMC6511868
OpenAlexW2921428813

What OpenQuestion holds

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LicenceCC BY
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.