Evidence map›Paper›PMID 33674615›Full record

ArticleNature communications2021

psiCLIP reveals dynamic RNA binding by DEAH-box helicases before and after exon ligation.

Lisa M Strittmatter, Charlotte Capitanchik, Andrew J Newman, Martina Hallegger, Christine M Norman, Sebastian M Fica, Chris Oubridge, Nicholas M Luscombe, Jernej Ule, Kiyoshi Nagai

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Control of 3' splice site selection by the yeast splicing factor Fyv6.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Structural studies of the spliceosome: Bridging the gaps.Current opinion in structural biology · 2022
    Review
  12. Article
  13. Article
  14. 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

10 authors at 4 institutions in 2 countries.

Lisa M Strittmatter *MRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0003-0206-3155
Charlotte Capitanchik *The Francis Crick Institute, London, UK.
Andrew J NewmanMRC Laboratory of Molecular Biology, Cambridge, UK.
Martina HalleggerThe Francis Crick Institute, London, UK.
Christine M NormanMRC Laboratory of Molecular Biology, Cambridge, UK.
Sebastian M FicaMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-9186-0361
Chris OubridgeMRC Laboratory of Molecular Biology, Cambridge, UK.
Nicholas M LuscombeThe Francis Crick Institute, London, UK.ORCID 0000-0001-5293-4778
Jernej UleThe Francis Crick Institute, London, UK. jernej.ule@crick.ac.uk.ORCID 0000-0002-2452-4277
Kiyoshi NagaiMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0003-1785-6510
MRC Laboratory of Molecular Biology · GBThe Francis Crick Institute · GBOkinawa Institute of Science and Technology Graduate University · JPQueen Mary University of London · GB

Funding

Cancer Research UK FC010110Medical Research Council FC010110Medical Research Council MC_U105184330Medical Research Council MR/L016311/1Wellcome TrustWellcome Trust 103760/Z/14/ZWellcome Trust FC010110
6 · The paper itself

Abstract

RNA helicases remodel the spliceosome to enable pre-mRNA splicing, but their binding and mechanism of action remain poorly understood. To define helicase-RNA contacts in specific spliceosomal states, we develop purified spliceosome iCLIP (psiCLIP), which reveals dynamic helicase-RNA contacts during splicing catalysis. The helicase Prp16 binds along the entire available single-stranded RNA region between the branchpoint and 3'-splice site, while Prp22 binds diffusely downstream of the branchpoint before exon ligation, but then switches to more narrow binding in the downstream exon after exon ligation, arguing against a mechanism of processive translocation. Depletion of the exon-ligation factor Prp18 destabilizes Prp22 binding to the pre-mRNA, suggesting that proofreading by Prp22 may sense the stability of the spliceosome during exon ligation. Thus, psiCLIP complements structural studies by providing key insights into the binding and proofreading activity of spliceosomal RNA helicases.

Indexed as

ExonsRNA SplicingAdenosine TriphosphatasesAutoantigensCryoelectron MicroscopyDEAD-box RNA HelicasesModels, MolecularRecombinant ProteinsRibonucleoproteins, Small NuclearRibonucleoprotein, U5 Small NuclearRNA, FungalRNA HelicasesRNA PrecursorsRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSpliceosomesAdenosine TriphosphatasesAutoantigensDEAD-box RNA HelicasesPRP16 protein, S cerevisiaePRP18 protein, S cerevisiaePRP22 protein, S cerevisiaeRecombinant ProteinsRibonucleoproteins, Small NuclearRibonucleoprotein, U5 Small NuclearRNA, FungalRNA HelicasesRNA PrecursorsRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSMB protein, S cerevisiae

Identifiers

PMID33674615
PMCPMC7935899
OpenAlexW3133619870

What OpenQuestion holds

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LicenceCC BY
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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.