Evidence map›Paper›PMID 9463390›Full record

ArticleThe EMBO journal1998

Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3' end formation of 5.8S rRNA in Saccharomyces cerevisiae.

J de la Cruz, D Kressler, D Tollervey, P Linder

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers.

0numbers the graph read from it
0cells of the map it votes in
179citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

179 citing papers in PubMed, 312 citations in OpenAlex.

  1. Review
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  6. RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026
    Review
  7. Article
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  11. Built differently or defective: can RNA exosomopathies cause ribosome heterogeneity?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  12. TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Yeast pre-rRNA is processed at the A' site.microPublication biology · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Evolution and Functional Roles ofInternational journal of molecular sciences · 2022
    Review

119 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

J de la CruzDépartement de Biochimie Médicale, Centre Médical Universitaire, Université de Genève, Switzerland. Jesus.Cruz@medecine.unige.ch
D Kressler
D Tollervey
P Linder
University of Geneva · CH

Funding

Wellcome Trust
6 · The paper itself

Abstract

The temperature-sensitive mutation, dob1-1, was identified in a screen for dependence on overexpression of the yeast translation initiation factor eIF4B (Tif3p). Dob1p is an essential putative ATP-dependent RNA helicase. Polysome analyses revealed an under accumulation of 60S ribosomal subunits in the dob1-1 mutant. Pulse-chase labelling of pre-rRNA showed that this was due to a defect in the synthesis of the 5.8S and 25S rRNAs. Northern and primer extension analyses in the dob1-1 mutant, or in a strain genetically depleted of Dob1p, revealed a specific inhibition of the 3' processing of the 5.8S rRNA from its 7S precursor. This processing recently has been attributed to the activity of the exosome, a complex of 3'-->5' exonucleases that includes Rrp4p. In vivo depletion of Dob1p also inhibits degradation of the 5' external transcribed spacer region of the pre-rRNA. A similar phenotype was observed in rrp4 mutant strains and, moreover, the dob1-1 and rrp4-1 mutations show a strong synergistic growth inhibition. We propose that Dob1p functions as a cofactor for the exosome complex that unwinds secondary structures in the pre-rRNA that otherwise block the progression of the 3'-->5' exonucleases.

Indexed as

Saccharomyces cerevisiae ProteinsCloning, MolecularDEAD-box RNA HelicasesEukaryotic Initiation FactorsExoribonucleasesFungal ProteinsGalactoseMutagenesisNuclear ProteinsPeptide Initiation FactorsPhenotypeRibosomal ProteinsRNA-Binding ProteinsRNA HelicasesRNA NucleotidyltransferasesRNA PrecursorsDEAD-box RNA HelicasesEukaryotic Initiation FactorsExoribonucleasesFungal ProteinsGalactoseMTR4 protein, S cerevisiaeNuclear ProteinsPeptide Initiation FactorsRibosomal ProteinsRNA-Binding ProteinsRNA HelicasesRNA NucleotidyltransferasesRNA PrecursorsRNA, Ribosomal, 5SRRP4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTIF3 protein, S cerevisiae

Identifiers

PMID9463390
PMCPMC1170461
OpenAlexW2110544609

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.