Evidence map›Paper›PMID 29880797›Full record

ArticleNature communications2018

Molecular principles underlying dual RNA specificity in the Drosophila SNF protein.

Gert Weber, Gregory T DeKoster, Nicole Holton, Kathleen B Hall, Markus C Wahl

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019
    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 3 institutions in 2 countries.

Gert WeberLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraße 6, D-14195, Berlin, Germany. gweber@posteo.de.ORCID http://orcid.org/0000-0003-3624-1060
Gregory T DeKosterDepartment of Biochemistry and Molecular Biophysics, Washington University Medical School, St. Louis, Missouri, 63110, USA.
Nicole HoltonLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraße 6, D-14195, Berlin, Germany.
Kathleen B HallDepartment of Biochemistry and Molecular Biophysics, Washington University Medical School, St. Louis, Missouri, 63110, USA. kathleenhal@gmail.com.
Markus C WahlLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraße 6, D-14195, Berlin, Germany. mwahl@zedat.fu-berlin.de.ORCID http://orcid.org/0000-0002-2811-5307
Helmholtz-Zentrum Berlin für Materialien und Energie · DEWashington University in St. Louis · USFreie Universität Berlin · DE

Funding

Coevolution of snrnp U1A/U2B proteins and snRNA stemloopsR01GM096444 · NIGMS · WASHINGTON UNIVERSITY · PI HALL, KATHLEEN B · 2011 to 2014
$1.4M
NIGMS NIH HHS R01 GM096444
6 · The paper itself

Abstract

The first RNA recognition motif of the Drosophila SNF protein is an example of an RNA binding protein with multi-specificity. It binds different RNA hairpin loops in spliceosomal U1 or U2 small nuclear RNAs, and only in the latter case requires the auxiliary U2A' protein. Here we investigate its functions by crystal structures of SNF alone and bound to U1 stem-loop II, U2A' or U2 stem-loop IV and U2A', SNF dynamics from NMR spectroscopy, and structure-guided mutagenesis in binding studies. We find that different loop-closing base pairs and a nucleotide exchange at the tips of the loops contribute to differential SNF affinity for the RNAs. U2A' immobilizes SNF and RNA residues to restore U2 stem-loop IV binding affinity, while U1 stem-loop II binding does not require such adjustments. Our findings show how U2A' can modulate RNA specificity of SNF without changing SNF conformation or relying on direct RNA contacts.

Indexed as

Amino Acid MotifsBinding SitesCrystallography, X-RayDrosophila ProteinsModels, MolecularMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularProtein BindingProtein DomainsRecombinant ProteinsRibonucleoprotein, U1 Small NuclearRibonucleoprotein, U2 Small NuclearRNA, Small NuclearSubstrate SpecificityDrosophila ProteinsRecombinant ProteinsRibonucleoprotein, U1 Small NuclearRibonucleoprotein, U2 Small NuclearRNA, Small Nuclearsnf protein, DrosophilaU1 small nuclear RNAU2A protein, DrosophilaU2 small nuclear RNA

Identifiers

PMID29880797
PMCPMC5992148
OpenAlexW2805349799

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.