Evidence map›Paper›PMID 23404585›Full record

ArticleNucleic acids research2013

The RNA exosome complex central channel controls both exonuclease and endonuclease Dis3 activities in vivo and in vitro.

Karolina Drazkowska, Rafal Tomecki, Krystian Stodus, Katarzyna Kowalska, Mariusz Czarnocki-Cieciura, Andrzej Dziembowski

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 58 citations in OpenAlex.

  1. Ribosome engineering enhances genetic code expansion inSynthetic and systems biotechnology · 2027
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  6. International journal of molecular sciences · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Substrate discrimination and quality control require each catalytic activity of TRAMP and the nuclear RNA exosome.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Article
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  14. Article
  15. RNA Exosomes and Their Cofactors.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
  16. Article
  17. Article
  18. 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

6 authors at 1 institution in 1 country.

Karolina DrazkowskaDepartment of Biophysics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Rafal Tomecki
Krystian Stodus
Katarzyna Kowalska
Mariusz Czarnocki-Cieciura
Andrzej Dziembowski
Polish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNA exosome is an essential ribonuclease complex involved in RNA processing and decay. It consists of a 9-subunit catalytically inert ring composed of six RNase PH-like proteins forming a central channel and three cap subunits with KH/S1 domains located at the top. The yeast exosome catalytic activity is supplied by the Dis3 (also known as Rrp44) protein, which has both endo- and exoribonucleolytic activities and the nucleus-specific exonuclease Rrp6. In vitro studies suggest that substrates reach the Dis3 exonucleolytic active site following passage through the ring channel, but in vivo support is lacking. Here, we constructed an Rrp41 ring subunit mutant with a partially blocked channel that led to thermosensitivity and synthetic lethality with Rrp6 deletion. Rrp41 mutation caused accumulation of nuclear and cytoplasmic exosome substrates including the non-stop decay reporter, for which degradation is dependent on either endonucleolytic or exonucleolytic Dis3 activities. This suggests that the central channel also controls endonucleolytic activity. In vitro experiments performed using Chaetomium thermophilum exosomes reconstituted from recombinant subunits confirmed this notion. Finally, we analysed the impact of a lethal mutation of conserved basic residues in Rrp4 cap subunit and found that it inhibits digestion of single-stranded and structured RNA substrates.

Indexed as

Cell NucleusChaetomiumCytoplasmExosome Multienzyme Ribonuclease ComplexGenes, LethalMutationPhenotypeRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDIS3 protein, S cerevisiaeExosome Multienzyme Ribonuclease ComplexRRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKI6 protein, S cerevisiae

Identifiers

PMID23404585
PMCPMC3616716
OpenAlexW2098474935

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.