Evidence map›Paper›PMID 12417728›Full record

ArticleMolecular and cellular biology2002

Interactions between mRNA export commitment, 3'-end quality control, and nuclear degradation.

Domenico Libri, Ken Dower, Jocelyne Boulay, Rune Thomsen, Michael Rosbash, Torben Heick Jensen

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

126 citing papers in PubMed, 247 citations in OpenAlex.

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  13. The mBiochimica et biophysica acta. Gene regulatory mechanisms · 2019
    Review
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  18. Controlling nuclear RNA levels.Nature reviews. Genetics · 2018
    Review
  19. Article
  20. Article

66 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

6 authors at 3 institutions in 3 countries.

Domenico LibriCentre National de la Recherche Scientifique, Centre de Genetique Moleculaire, 91190 Gif-sur-Yvette, France. Libri@cgm.cnrs-gif.fr
Ken Dower
Jocelyne Boulay
Rune Thomsen
Michael Rosbash
Torben Heick Jensen
Aarhus University · DKBrandeis University · USCentre de Génétique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several aspects of eukaryotic mRNA processing are linked to transcription. In Saccharomyces cerevisiae, overexpression of the mRNA export factor Sub2p suppresses the growth defect of hpr1 null cells, yet the protein Hpr1p and the associated THO protein complex are implicated in transcriptional elongation. Indeed, we find that a pool of heat shock HSP104 transcripts are 3'-end truncated in THO complex mutant as well as sub2 mutant backgrounds. Surprisingly, however, this defect can be suppressed by deletion of the 3'-5' exonuclease Rrp6p. This indicates that incomplete RNAs result from nuclear degradation rather than from a failure to efficiently elongate transcription. RNAs that are not degraded are retained at the transcription site in a Rrp6p-dependent manner. Interestingly, the addition of a RRP6 deletion to sub2 or to THO complex mutants shows a strong synthetic growth phenotype, suggesting that the failure to retain and/or degrade defective mRNAs is deleterious. mRNAs produced in the 3'-end processing mutants rna14-3 and rna15-2, as well as an RNA harboring a 3' end generated by a self-cleaving hammerhead ribozyme, are also retained in Rrp6p-dependent transcription site foci. Taken together, our results show that several classes of defective RNPs are subject to a quality control step that impedes release from transcription site foci and suggest that suboptimal messenger ribonucleoprotein assembly leads to RNA degradation by Rrp6p.

Indexed as

ExoribonucleasesActive Transport, Cell NucleusAdenosine TriphosphatasesCell NucleusExosome Multienzyme Ribonuclease ComplexFungal ProteinsGenes, FungalHeat-Shock ProteinsMacromolecular SubstancesNuclear ProteinsRNA 3' End ProcessingRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticAdenosine TriphosphatasesExoribonucleasesExosome Multienzyme Ribonuclease ComplexFungal ProteinsHeat-Shock ProteinsHPR1 protein, S cerevisiaeHsP104 protein, S cerevisiaeMacromolecular SubstancesNuclear ProteinsRNA-dependent ATPaseRNA, MessengerRRP6 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID12417728
PMCPMC134070
OpenAlexW2100041522

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.