Evidence map›Paper›PMID 17704127›Full record

ArticleNucleic acids research2007

The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein.

Jonathan A Stead, Joe L Costello, Michaela J Livingstone, Phil Mitchell

Abstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Polyadenylated versions of small non-coding RNAs inMicrobial cell (Graz, Austria) · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. RNA Exosomes and Their Cofactors.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
  18. Reconstitution of the Schizosaccharomyces pombe RNA Exosome.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  19. Article
  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

4 authors.

Jonathan A SteadDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Joe L Costello
Michaela J Livingstone
Phil Mitchell

Funding

Biotechnology and Biological Sciences Research Council BB/D001161/1
6 · The paper itself

Abstract

The exosome complex is a key component of the cellular RNA surveillance machinery and is required for normal 3' end processing of many stable RNAs. Exosome activity requires additional factors such as the Ski or TRAMP complexes to activate the complex or facilitate substrate binding. Rrp47p promotes the catalytic activity of the exosome component Rrp6p, but its precise function is unknown. Here we show that recombinant Rrp47p is expressed as an apparently hexameric complex that specifically binds structured nucleic acids. Furthermore, pull-down assays demonstrated that Rrp47p interacts directly with the N-terminal region of Rrp6p that contains the functionally uncharacterized PMC2NT domain. Strains expressing a mutant form of Rrp6p lacking the N-terminal region failed to accumulate Rrp47p at normal levels, exhibited a slow growth phenotype characteristic of rrp47-Delta mutants and showed RNA processing defects consistent with loss of Rrp47p function. These findings suggest Rrp47p promotes Rrp6p activity by facilitating binding via the PMC2NT domain to structural elements within RNA. Notably, characterized Rrp6p substrates such as the 5.8S+30 species are predicted to contain helices at their 3' termini, while others such as intergenic or antisense cryptic unstable transcripts could potentially form extensive double-stranded molecules with overlapping mRNAs.

Indexed as

RNA 3' End ProcessingDNADNA-Binding ProteinsExoribonucleasesExosome Multienzyme Ribonuclease ComplexNuclear ProteinsProtein Structure, TertiaryRNARNA-Binding ProteinsRNA, Ribosomal, 5.8SRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNADNA-Binding ProteinsExoribonucleasesExosome Multienzyme Ribonuclease ComplexLRP1 protein, S cerevisiaeNuclear ProteinsRNARNA-Binding ProteinsRNA, Ribosomal, 5.8SRNA, Small NucleolarRRP6 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID17704127
PMCPMC2018643

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Registered trials

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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.