Evidence map›Paper›PMID 19060898›Full record

ArticleNature structural & molecular biology2009

The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities.

Daneen Schaeffer, Borislava Tsanova, Ana Barbas, Filipa Pereira Reis, Eeshita Ghosh Dastidar, Maya Sanchez-Rotunno, Cecília Maria Arraiano, Ambro van Hoof

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers.

0numbers the graph read from it
0cells of the map it votes in
177citing 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

177 citing papers in PubMed.

  1. Review
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  6. Formation of Circular RNAs.Advances in experimental medicine and biology · 2025
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  8. Advances in Engineering Circular RNA Vaccines.Pathogens (Basel, Switzerland) · 2024
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  9. Article
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  13. Article
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  15. Review
  16. International journal of molecular sciences · 2023
    Review
  17. Article
  18. Circular RNAs in vascular diseases.Frontiers in cardiovascular medicine · 2023
    Review
  19. Control of RNA degradation in cell fate decision.Frontiers in cell and developmental biology · 2023
    Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Daneen SchaefferDepartment of Microbiology and Molecular Genetics, University of Texas Health Science Center-Houston, 6431 Fannin Street, MSB 1.212 Houston, Texas 77030, USA.
Borislava Tsanova
Ana Barbas
Filipa Pereira Reis
Eeshita Ghosh Dastidar
Maya Sanchez-Rotunno
Cecília Maria Arraiano
Ambro van Hoof

Funding

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 R01 GM069900
6 · The paper itself

Abstract

The eukaryotic exosome is a ten-subunit 3' exoribonucleolytic complex responsible for many RNA-processing and RNA-degradation reactions. How the exosome accomplishes this is unknown. Rrp44 (also known as Dis3), a member of the RNase II family of enzymes, is the catalytic subunit of the exosome. We show that the PIN domain of Rrp44 has endoribonucleolytic activity. The PIN domain is preferentially active toward RNA with a 5' phosphate, suggesting coordination of 5' and 3' processing. We also show that the endonuclease activity is important in vivo. Furthermore, the essential exosome subunit Csl4 does not contain any domains that are required for viability, but its zinc-ribbon domain is required for exosome-mediated mRNA decay. These results suggest that specific exosome domains contribute to specific functions, and that different RNAs probably interact with the exosome differently. The combination of an endoRNase and an exoRNase activity seems to be a widespread feature of RNA-degrading machines.

Indexed as

AnimalsCatalytic DomainCytoplasmEndoribonucleasesExoribonucleasesExosome Multienzyme Ribonuclease ComplexExosomesHumansPeptide FragmentsRibonucleasesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDIS3 protein, S cerevisiaeEndoribonucleasesExoribonucleasesExosome Multienzyme Ribonuclease ComplexPeptide FragmentsRibonucleasesRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID19060898
PMCPMC2615074

What OpenQuestion holds

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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.