Evidence map›Paper›PMID 24224060›Full record

ArticlePloS one2013

The exosome cofactor Rrp47 is critical for the stability and normal expression of its associated exoribonuclease Rrp6 in Saccharomyces cerevisiae.

Monika Feigenbutz, William Garland, Martin Turner, Phil Mitchell

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Reconstitution of the Human Nuclear RNA Exosome.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  11. Reconstitution of the Schizosaccharomyces pombe RNA Exosome.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  12. RNA Exosomes and Their Cofactors.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Stress-induced nuclear depletion ofThe Journal of biological chemistry · 2018
    Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Monika FeigenbutzMolecular Biology and Biotechnology Department, The University of Sheffield, Sheffield, United Kingdom.
William Garland
Martin Turner
Phil Mitchell
University of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome TrustWellcome Trust 08836/Z/09/Z
6 · The paper itself

Abstract

Rrp6 is a conserved catalytic subunit of the eukaryotic nuclear exosome ribonuclease complex that functions in the productive 3' end maturation of stable RNAs, the degradation of transiently expressed noncoding transcripts and in discard pathways that eradicate the cell of incorrectly processed or assembled RNAs. The function of Rrp6 in these pathways is at least partially dependent upon its interaction with a small nuclear protein called Rrp47/Lrp1, but the underlying mechanism(s) by which Rrp47 functions in concert with Rrp6 are not established. Previous work on yeast grown in rich medium has suggested that Rrp6 expression is not markedly reduced in strains lacking Rrp47. Here we show that Rrp6 expression in rrp47∆ mutants is substantially reduced during growth in minimal medium through effects on both transcript levels and protein stability. Exogenous expression of Rrp6 enables normal levels to be attained in rrp47∆ mutants. Strikingly, exogenous expression of Rrp6 suppresses many, but not all, of the RNA processing and maturation defects observed in an rrp47∆ mutant and complements the synthetic lethality of rrp47∆ mpp6∆ and rrp47∆ rex1∆ double mutants. Increased Rrp6 expression in the resultant rrp47∆ rex1∆ double mutant suppresses the defect in the 3' maturation of box C/D snoRNAs. In contrast, increased Rrp6 expression in the rrp47∆ mpp6∆ double mutant diminishes the block in the turnover of CUTs and in the degradation of the substrates of RNA discard pathways. These results demonstrate that a principal function of Rrp47 is to facilitate appropriate expression levels of Rrp6 and support the conclusion that the Rrp6/Rrp47 complex and Rex1 provide redundant exonuclease activities for the 3' end maturation of box C/D snoRNAs.

Indexed as

DNA-Binding ProteinsExosome Multienzyme Ribonuclease ComplexNuclear ProteinsProtein StabilityRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsExosome Multienzyme Ribonuclease ComplexLRP1 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsRRP6 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID24224060
PMCPMC3818262
OpenAlexW2155719221

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.