Evidence map›Paper›PMID 27995908›Full record

ArticleNature communications2016

Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution.

Tarek Hilal, Hiroshi Yamamoto, Justus Loerke, Jörg Bürger, Thorsten Mielke, Christian M T Spahn

Abstract read
In one paragraph

Article in Nature communications, 2016. 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
–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

39 citing papers in PubMed.

  1. Article
  2. RNAViruses · 2026
    Review
  3. Article
  4. Review
  5. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A ubiquitin language communicates ribosomal distress.Seminars in cell & developmental biology · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Rebirth of the translational machinery: The importance of recycling ribosomes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  19. Review
  20. 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

6 authors.

Tarek HilalInstitut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Hiroshi YamamotoInstitut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Justus LoerkeInstitut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Jörg BürgerInstitut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
Thorsten MielkeMax-Planck Institut für Molekulare Genetik, Ihnestrasse 63-73, 14195 Berlin, Germany.ORCID 0000-0001-9275-3146
Christian M T SpahnInstitut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The surveillance of mRNA translation is imperative for homeostasis. Monitoring the integrity of the message is essential, as the translation of aberrant mRNAs leads to stalling of the translational machinery. During ribosomal rescue, arrested ribosomes are specifically recognized by the conserved eukaryotic proteins Dom34 and Hbs1, to initiate their recycling. Here we solve the structure of Dom34 and Hbs1 bound to a yeast ribosome programmed with a nonstop mRNA at 3.3 Å resolution using cryo-electron microscopy. The structure shows that Domain N of Dom34 is inserted into the upstream mRNA-binding groove via direct stacking interactions with conserved nucleotides of 18S rRNA. It senses the absence of mRNA at the A-site and part of the mRNA entry channel by direct competition. Thus, our analysis establishes the structural foundation for the recognition of aberrantly stalled 80S ribosomes by the Dom34·Hbs1·GTP complex during Dom34-mediated mRNA surveillance pathways.

Indexed as

Cell Cycle ProteinsCryoelectron MicroscopyEndoribonucleasesGTP-Binding ProteinsGuanylyl ImidodiphosphateHSP70 Heat-Shock ProteinsModels, MolecularPeptide Elongation FactorsProtein DomainsProtein Interaction Domains and MotifsRecombinant ProteinsRibosomesRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsDom34 protein, S cerevisiaeEndoribonucleasesGTP-Binding ProteinsGuanylyl ImidodiphosphateHBS1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsPeptide Elongation FactorsRecombinant ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID27995908
PMCPMC5187420

What OpenQuestion holds

Textmetadata
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.