Evidence map›Paper›PMID 26673105›Full record

ArticleRNA (New York, N.Y.)2016

Multiple protein-protein interactions converging on the Prp38 protein during activation of the human spliceosome.

Tonio Schütze, Alexander K C Ulrich, Luise Apelt, Cindy L Will, Natascha Bartlick, Martin Seeger, Gert Weber, Reinhard Lührmann, Ulrich Stelzl, Markus C Wahl

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

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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.

Tonio SchützeFreie Universität Berlin, Laboratory of Structural Biochemistry, D-14195 Berlin, Germany.
Alexander K C UlrichFreie Universität Berlin, Laboratory of Structural Biochemistry, D-14195 Berlin, Germany.
Luise ApeltMax-Planck Institute for Molecular Genetics, Otto-Warburg Laboratory, D-14195 Berlin, Germany.
Cindy L WillMax Planck Institute for Biophysical Chemistry, Department of Cellular Biochemistry, D-37077 Göttingen, Germany.
Natascha BartlickFreie Universität Berlin, Laboratory of Structural Biochemistry, D-14195 Berlin, Germany.
Martin SeegerFreie Universität Berlin, Laboratory of Structural Biochemistry, D-14195 Berlin, Germany.
Gert WeberFreie Universität Berlin, Laboratory of Structural Biochemistry, D-14195 Berlin, Germany.
Reinhard LührmannMax Planck Institute for Biophysical Chemistry, Department of Cellular Biochemistry, D-37077 Göttingen, Germany.
Ulrich StelzlMax-Planck Institute for Molecular Genetics, Otto-Warburg Laboratory, D-14195 Berlin, Germany University of Graz, Institute of Pharmaceutical Sciences (IPW), Pharmaceutical Chemistry, A-8010 Graz, Austria.
Markus C WahlFreie Universität Berlin, Laboratory of Structural Biochemistry, D-14195 Berlin, Germany.
Freie Universität Berlin · DEMax Planck Institute for Biophysical Chemistry · DEMax Planck Institute for Molecular Genetics · DEUniversity of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spliceosomal Prp38 proteins contain a conserved amino-terminal domain, but only higher eukaryotic orthologs also harbor a carboxy-terminal RS domain, a hallmark of splicing regulatory SR proteins. We show by crystal structure analysis that the amino-terminal domain of human Prp38 is organized around three pairs of antiparallel α-helices and lacks similarities to RNA-binding domains found in canonical SR proteins. Instead, yeast two-hybrid analyses suggest that the amino-terminal domain is a versatile protein-protein interaction hub that possibly binds 12 other spliceosomal proteins, most of which are recruited at the same stage as Prp38. By quantitative, alanine surface-scanning two-hybrid screens and biochemical analyses we delineated four distinct interfaces on the Prp38 amino-terminal domain. In vitro interaction assays using recombinant proteins showed that Prp38 can bind at least two proteins simultaneously via two different interfaces. Addition of excess Prp38 amino-terminal domain to in vitro splicing assays, but not of an interaction-deficient mutant, stalled splicing at a precatalytic stage. Our results show that human Prp38 is an unusual SR protein, whose amino-terminal domain is a multi-interface protein-protein interaction platform that might organize the relative positioning of other proteins during splicing.

Indexed as

RNA SplicingAmino Acid SequenceAnimalsArabidopsisBinding SitesCrystallography, X-RayEscherichia coliGene ExpressionHumansModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsProtein SubunitsPRP38 protein, S cerevisiaeRecombinant ProteinsRNA, MessengerRNA PrecursorsRNA Splicing FactorsSaccharomyces cerevisiae Proteinspre-mRNA processing factor 38pre-mRNA splicingprotein–protein interactionsspliceosomal B complexspliceosomeyeast two-hybrid analysis

Identifiers

PMID26673105
PMCPMC4712676
OpenAlexW2282402804

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.