Evidence map›Paper›PMID 28838205›Full record

ArticleNucleic acids research2017

A new role for FBP21 as regulator of Brr2 helicase activity.

Lisa M Henning, Karine F Santos, Jana Sticht, Stefanie Jehle, Chung-Tien Lee, Malte Wittwer, Henning Urlaub, Ulrich Stelzl, Markus C Wahl, Christian Freund

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  14. Structural Insights into Nuclear pre-mRNA Splicing in Higher Eukaryotes.Cold Spring Harbor perspectives in biology · 2019
    Review
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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 1 country.

Lisa M HenningLaboratory of Protein Biochemistry, Institute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, Berlin 14195, Germany.
Karine F SantosLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustr. 6, Berlin 14195, Germany.
Jana StichtLaboratory of Protein Biochemistry, Institute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, Berlin 14195, Germany.
Stefanie JehleMax-Planck-Insitute for Molecular Genetics, Ihnestraße 63-74, Berlin 14195, Germany.
Chung-Tien LeeMax-Planck-Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry Group, Am Fassberg 11, Göttingen 37077, Germany.
Malte WittwerLaboratory of Protein Biochemistry, Institute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, Berlin 14195, Germany.
Henning UrlaubMax-Planck-Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry Group, Am Fassberg 11, Göttingen 37077, Germany.
Ulrich StelzlMax-Planck-Insitute for Molecular Genetics, Ihnestraße 63-74, Berlin 14195, Germany.
Markus C WahlLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustr. 6, Berlin 14195, Germany.
Christian FreundLaboratory of Protein Biochemistry, Institute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, Berlin 14195, Germany.
Freie Universität Berlin · DEMax Planck Institute for Biophysical Chemistry · DEMax Planck Institute for Molecular Genetics · DEHelmholtz-Zentrum Berlin für Materialien und Energie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Splicing of eukaryotic pre-mRNA is carried out by the spliceosome, which assembles stepwise on each splicing substrate. This requires the concerted action of snRNPs and non-snRNP accessory proteins, the functions of which are often not well understood. Of special interest are B complex factors that enter the spliceosome prior to catalytic activation and may alter splicing kinetics and splice site selection. One of these proteins is FBP21, for which we identified several spliceosomal binding partners in a yeast-two-hybrid screen, among them the RNA helicase Brr2. Biochemical and biophysical analyses revealed that an intrinsically disordered region of FBP21 binds to an extended surface of the C-terminal Sec63 unit of Brr2. Additional contacts in the C-terminal helicase cassette are required for allosteric inhibition of Brr2 helicase activity. Furthermore, the direct interaction between FBP21 and the U4/U6 di-snRNA was found to reduce the pool of unwound U4/U6 di-snRNA. Our results suggest FBP21 as a novel key player in the regulation of Brr2.

Indexed as

Allosteric RegulationAmino Acid SequenceCarrier ProteinsHumansModels, MolecularNuclear ProteinsPeptide FragmentsProtein BindingProtein Interaction Domains and MotifsRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA HelicasesRNA PrecursorsRNA, Small NuclearRNA SplicingSaccharomyces cerevisiae ProteinsCarrier ProteinsNuclear ProteinsPeptide FragmentsRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA HelicasesRNA PrecursorsRNA, Small NuclearSaccharomyces cerevisiae ProteinsSNRNP200 protein, humanU4 small nuclear RNAU6 small nuclear RNAWBP4 protein, human

Identifiers

PMID28838205
PMCPMC5570060
OpenAlexW2729522052

What OpenQuestion holds

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LicenceCC BY-NC
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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.