Evidence map›Paper›PMID 26161500›Full record

ArticleeLife2015

A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing.

Sunbin Liu, Sina Mozaffari-Jovin, Jan Wollenhaupt, Karine F Santos, Matthias Theuser, Stanislaw Dunin-Horkawicz, Patrizia Fabrizio, Janusz M Bujnicki, Reinhard Lührmann, Markus C Wahl

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 38 citations in OpenAlex.

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  16. Substrate-assisted mechanism of RNP disruption by the spliceosomal Brr2 RNA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Conserved structure of Snu13 from the highly reduced spliceosome of Cyanidioschyzon merolae.Protein science : a publication of the Protein Society · 2016
    Article
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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.

Sunbin LiuLaboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
Sina Mozaffari-JovinDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Jan WollenhauptLaboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
Karine F SantosLaboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
Matthias TheuserLaboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
Stanislaw Dunin-HorkawiczLaboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, Warsaw, Poland.
Patrizia FabrizioDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Janusz M BujnickiLaboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, Warsaw, Poland.
Reinhard LührmannDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Markus C WahlLaboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
Freie Universität Berlin · DEMax Planck Institute for Biophysical Chemistry · DEAdam Mickiewicz University in Poznań · PLInternational Institute of Molecular and Cell Biology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prp3 is an essential U4/U6 di-snRNP-associated protein whose functions and molecular mechanisms in pre-mRNA splicing are presently poorly understood. We show by structural and biochemical analyses that Prp3 contains a bipartite U4/U6 di-snRNA-binding region comprising an expanded ferredoxin-like fold, which recognizes a 3'-overhang of U6 snRNA, and a preceding peptide, which binds U4/U6 stem II. Phylogenetic analyses revealed that the single-stranded RNA-binding domain is exclusively found in Prp3 orthologs, thus qualifying as a spliceosome-specific RNA interaction module. The composite double-stranded/single-stranded RNA-binding region assembles cooperatively with Snu13 and Prp31 on U4/U6 di-snRNAs and inhibits Brr2-mediated U4/U6 di-snRNA unwinding in vitro. RNP-disrupting mutations in Prp3 lead to U4/U6•U5 tri-snRNP assembly and splicing defects in vivo. Our results reveal how Prp3 acts as an important bridge between U4/U6 and U5 in the tri-snRNP and comparison with a Prp24-U6 snRNA recycling complex suggests how Prp3 may be involved in U4/U6 reassembly after splicing.

Indexed as

RNA SplicingCrystallography, X-RayDNA Mutational AnalysisHumansModels, BiologicalModels, MolecularMutationNuclear ProteinsProtein BindingRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNANuclear ProteinsPRPF3 protein, humanRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNAbiochemistrybiophysicshumanpre-mRNA splicingprotein–RNA interactionS. cerevisiaesmall nuclear ribonucleoprotein particlestructural biologyX-ray crystallography

Identifiers

PMID26161500
PMCPMC4520091
OpenAlexW2121591967

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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.