Evidence map›Paper›PMID 22833611›Full record

ArticleNucleic acids research2012

The CR3 motif of Rrp44p is important for interaction with the core exosome and exosome function.

Daneen Schaeffer, Filipa Pereira Reis, Sean J Johnson, Cecília Maria Arraiano, Ambro van Hoof

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Review
  2. International journal of molecular sciences · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Looking into the barrel of the RNA exosome.Nature structural & molecular biology · 2014
    Article
  18. Threading the barrel of the RNA exosome.Trends in biochemical sciences · 2013
    Review
  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

5 authors.

Daneen SchaefferDepartment of Microbiology and Molecular Genetics, University of Texas Health Science Center-Houston, Houston, TX 77030, USA.
Filipa Pereira Reis
Sean J Johnson
Cecília Maria Arraiano
Ambro van Hoof

Funding

RNA decay and processing activities of the RNA exosomeR01GM099790 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI VAN HOOF, AMBRO · 2012 to 2020
$2.6M
METABOLISM OF YEAST mRNAS THAT LACK A STOP CODONR01GM069900 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI VAN HOOF, AMBRO · 2005 to 2009
$1.4M
NIGMS NIH HHS GM069900NIGMS NIH HHS GM099790NIGMS NIH HHS R01 GM099790
6 · The paper itself

Abstract

The 10-subunit RNA exosome is involved in a large number of diverse RNA processing and degradation events in eukaryotes. These reactions are carried out by the single catalytic subunit, Rrp44p/Dis3p, which is composed of three parts that are conserved throughout eukaryotes. The exosome is named for the 3' to 5' exoribonuclease activity provided by a large C-terminal region of the Rrp44p subunit that resembles other exoribonucleases. Rrp44p also contains an endoribonuclease domain. Finally, the very N-terminus of Rrp44p contains three Cys residues (CR3 motif) that are conserved in many eukaryotes but have no known function. These three conserved Cys residues cluster with a previously unrecognized conserved His residue in what resembles a metal-ion-binding site. Genetic and biochemical data show that this CR3 motif affects both endo- and exonuclease activity in vivo and both the nuclear and cytoplasmic exosome, as well as the ability of Rrp44p to associate with the other exosome subunits. These data provide the first direct evidence that the exosome-Rrp44p interaction is functionally important and also provides a molecular explanation for the functional defects when the conserved Cys residues are mutated.

Indexed as

CysteineEndoribonucleasesExosome Multienzyme Ribonuclease ComplexHistidineMutationProtein Interaction Domains and MotifsSaccharomyces cerevisiae ProteinsCysteineDIS3 protein, S cerevisiaeEndoribonucleasesExosome Multienzyme Ribonuclease ComplexHistidineSaccharomyces cerevisiae Proteins

Identifiers

PMID22833611
PMCPMC3467083

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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.