Evidence map›Paper›PMID 26503251›Full record

ArticleNucleic acids research2015

Assembly and dynamics of the U4/U6 di-snRNP by single-molecule FRET.

John W Hardin, Chandani Warnasooriya, Yasushi Kondo, Kiyoshi Nagai, David Rueda

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Microbiology (Reading, England) · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structure of the human 20S U5 snRNP.Nature structural & molecular biology · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

5 authors at 2 institutions in 1 country.

John W HardinDepartment of Medicine, Section of Virology, Imperial College London, London W12 0NN, UK Single Molecule Imaging Group, MRC Clinical Sciences Centre, Imperial College London, London W12 0NN, UK MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Chandani WarnasooriyaDepartment of Medicine, Section of Virology, Imperial College London, London W12 0NN, UK Single Molecule Imaging Group, MRC Clinical Sciences Centre, Imperial College London, London W12 0NN, UK.
Yasushi KondoMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Kiyoshi NagaiMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK kn@mrc-lmb.cam.ac.uk.
David RuedaDepartment of Medicine, Section of Virology, Imperial College London, London W12 0NN, UK Single Molecule Imaging Group, MRC Clinical Sciences Centre, Imperial College London, London W12 0NN, UK david.rueda@imperial.ac.uk.
Imperial College London · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC-A658-5TY10Medical Research Council MC U105184330Medical Research Council MC_U105184330Medical Research Council MC_UP_1102/5
6 · The paper itself

Abstract

In large ribonucleoprotein machines, such as ribosomes and spliceosomes, RNA functions as an assembly scaffold as well as a critical catalytic component. Protein binding to the RNA scaffold can induce structural changes, which in turn modulate subsequent binding of other components. The spliceosomal U4/U6 di-snRNP contains extensively base paired U4 and U6 snRNAs, Snu13, Prp31, Prp3 and Prp4, seven Sm and seven LSm proteins. We have studied successive binding of all protein components to the snRNA duplex during di-snRNP assembly by electrophoretic mobility shift assay and accompanying conformational changes in the U4/U6 RNA 3-way junction by single-molecule FRET. Stems I and II of the duplex were found to co-axially stack in free RNA and function as a rigid scaffold during the entire assembly, but the U4 snRNA 5' stem-loop adopts alternative orientations each stabilized by Prp31 and Prp3/4 binding accounting for altered Prp3/4 binding affinities in presence of Prp31.

Indexed as

Fluorescence Resonance Energy TransferNucleic Acid ConformationProtein BindingProtein Serine-Threonine KinasesRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSpliceosomesProtein Serine-Threonine KinasesPRP31 protein, S cerevisiaePRP4 protein, S cerevisiaeRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSnu13 protein, S cerevisiae

Identifiers

PMID26503251
PMCPMC4678811
OpenAlexW1844679536

What OpenQuestion holds

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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.