Evidence map›Paper›PMID 28355211›Full record

ArticlePLoS genetics2017

Transcriptome-wide analysis of alternative routes for RNA substrates into the exosome complex.

Clémentine Delan-Forino, Claudia Schneider, David Tollervey

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. RiboCop surveils pre-rRNA processing by Dicer in cellular quiescence.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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
  15. Article
  16. Article
  17. Article
  18. RNA Exosomes and Their Cofactors.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
  19. Article
  20. Mapping Exosome-Substrate Interactions In Vivo by UV Cross-Linking.Methods in molecular biology (Clifton, N.J.) · 2020
    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

3 authors at 2 institutions in 1 country.

Clémentine Delan-ForinoWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, United Kingdom.ORCID 0000-0003-0915-1211
Claudia SchneiderInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.ORCID 0000-0001-5597-2489
David TollerveyWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, United Kingdom.ORCID 0000-0003-2894-2772
Wellcome Centre for Cell Biology · GBNewcastle University · GB

Funding

Wellcome Trust 077248Wellcome Trust 092076
6 · The paper itself

Abstract

The RNA exosome complex functions in both the accurate processing and rapid degradation of many classes of RNA. Functional and structural analyses indicate that RNA can either be threaded through the central channel of the exosome or more directly access the active sites of the ribonucleases Rrp44 and Rrp6, but it was unclear how many substrates follow each pathway in vivo. We used CRAC (UV crosslinking and analysis of cDNA) in growing cells to identify transcriptome-wide interactions of RNAs with the major nuclear exosome-cofactor Mtr4 and with individual exosome subunits (Rrp6, Csl4, Rrp41 and Rrp44) along the threaded RNA path. We compared exosome complexes lacking Rrp44 exonuclease activity, carrying a mutation in the Rrp44 S1 RNA-binding domain predicted to disfavor direct access, or with multiple mutations in Rrp41 reported to impede RNA access to the central channel in vitro. Preferential use of channel-threading was seen for mRNAs, 5S rRNA, scR1 (SRP) and aborted tRNAs transcripts. Conversely, pre-tRNAs preferentially accessed Rrp44 directly. Both routes participated in degradation and maturation of RNAPI transcripts, with hand-over during processing. Rrp41 mutations blocked substrate passage through the channel to Rrp44 only for cytoplasmic mRNAs, supporting the predicted widening of the lumen in the Rrp6-associated, nuclear complex. Many exosome substrates exhibited clear preferences for a specific path to Rrp44. Other targets showed redundancy, possibly allowing the efficient handling of highly diverse RNA-protein complexes and RNA structures. Both threading and direct access routes involve the RNA helicase Mtr4. mRNAs that are predominately nuclear or cytoplasmic exosome substrates can be distinguished in vivo.

Indexed as

Catalytic DomainDEAD-box RNA HelicasesExosome Multienzyme Ribonuclease ComplexExosomesGene Expression ProfilingGene Expression RegulationNuclear ProteinsRNARNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptomeCSL4 protein, S cerevisiaeDEAD-box RNA HelicasesDIS3 protein, S cerevisiaeExosome Multienzyme Ribonuclease ComplexMTR4 protein, S cerevisiaeNuclear ProteinsRNARNA, MessengerRRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKI6 protein, S cerevisiae

Identifiers

PMID28355211
PMCPMC5389853
OpenAlexW2598909039

What OpenQuestion holds

Textmetadata
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.