Evidence map›Paper›PMID 21102444›Full record

ArticleNature structural & molecular biology2010

Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways.

Antonia M G van den Elzen, Julien Henri, Noureddine Lazar, María Eugenia Gas, Dominique Durand, François Lacroute, Magali Nicaise, Herman van Tilbeurgh, Bertrand Séraphin, Marc Graille

Open access · greenAbstract read
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In one paragraph

Article in Nature structural & molecular biology, 2010. 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
3.2field-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, 68 citations in OpenAlex.

  1. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
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  13. Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  14. Article
  15. Article
  16. Review
  17. RNA (New York, N.Y.) · 2017
    Article
  18. Article
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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

10 authors at 5 institutions in 1 country.

Antonia M G van den ElzenEquipe Labellisée La Ligue, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGMBC), Illkirch, France.
Julien Henri
Noureddine Lazar
María Eugenia Gas
Dominique Durand
François Lacroute
Magali Nicaise
Herman van Tilbeurgh
Bertrand Séraphin
Marc Graille
Centre National de la Recherche Scientifique · FRCentre de Génétique Moléculaire · FRUniversité Paris-Sud · FRInserm · FRInstitut de génétique et de biologie moléculaire et cellulaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cells have several quality control pathways that rely on translation to detect and degrade defective RNAs. Dom34 and Hbs1 are two proteins that are related to translation termination factors and are involved in no-go decay (NGD) and nonfunctional 18S ribosomal RNA (rRNA) decay (18S NRD) pathways that eliminate RNAs that cause strong ribosomal stalls. Here we present the structure of Hbs1 with and without GDP and a low-resolution model of the Dom34-Hbs1 complex. This complex mimics complexes of the elongation factor and transfer RNA or of the translation termination factors eRF1 and eRF3, supporting the idea that it binds to the ribosomal A-site. We show that nucleotide binding by Hbs1 is essential for NGD and 18S NRD. Mutations in Hbs1 that disrupted the interaction between Dom34 and Hbs1 strongly impaired NGD but had almost no effect on 18S NRD. Hence, NGD and 18S NRD could be genetically uncoupled, suggesting that mRNA and rRNA in a stalled translation complex may not always be degraded simultaneously.

Indexed as

Binding SitesCell Cycle ProteinsCrystallography, X-RayEndoribonucleasesGTP-Binding ProteinsHSP70 Heat-Shock ProteinsModels, MolecularMutationPeptide Elongation FactorsProtein Structure, TertiaryRNA, Ribosomal, 18SRNA StabilitySaccharomyces cerevisiae ProteinsScattering, Small AngleX-Ray DiffractionCell Cycle ProteinsDom34 protein, S cerevisiaeEndoribonucleasesGTP-Binding ProteinsHBS1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsPeptide Elongation FactorsRNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID21102444
OpenAlexW2034246870

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.