Evidence map›Paper›PMID 27115347›Full record

ArticleeLife2016

The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction.

Jean-Baptiste Fourmann, Olexandr Dybkov, Dmitry E Agafonov, Marcel J Tauchert, Henning Urlaub, Ralf Ficner, Patrizia Fabrizio, Reinhard Lührmann

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 55 citations in OpenAlex.

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  7. Cancer-associated SF3B1 mutation K700E causes widespread changes in U2/branchpoint recognition without altering splicing.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  15. DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1 in cancer.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  16. Regulation of the DEAH/RHA helicase Prp43 by the G-patch factor Pfa1.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

8 authors at 3 institutions in 1 country.

Jean-Baptiste FourmannDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
Olexandr DybkovDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
Dmitry E AgafonovDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
Marcel J TauchertDepartment of Molecular Structure Biology, Institute for Microbiology and Genetics, Georg August University of Göttingen, Göttingen, Germany.
Henning UrlaubBionalytics, Institute for Clinical Chemistry, University Medical Center Göttingen, Göttingen, Germany.
Ralf FicnerDepartment of Molecular Structure Biology, Institute for Microbiology and Genetics, Georg August University of Göttingen, Göttingen, Germany.
Patrizia FabrizioDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
Reinhard LührmannDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-6403-4432
Max Planck Institute for Biophysical Chemistry · DEUniversity of Göttingen · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DEAH-box NTPase Prp43 and its cofactors Ntr1 and Ntr2 form the NTR complex and are required for disassembling intron-lariat spliceosomes (ILS) and defective earlier spliceosomes. However, the Prp43 binding site in the spliceosome and its target(s) are unknown. We show that Prp43 fused to Ntr1's G-patch motif (Prp43_Ntr1GP) is as efficient as the NTR in ILS disassembly, yielding identical dissociation products and recognizing its natural ILS target even in the absence of Ntr1's C-terminal-domain (CTD) and Ntr2. Unlike the NTR, Prp43_Ntr1GP disassembles earlier spliceosomal complexes (A, B, B(act)), indicating that Ntr2/Ntr1-CTD prevents NTR from disrupting properly assembled spliceosomes other than the ILS. The U2 snRNP-intron interaction is disrupted in all complexes by Prp43_Ntr1GP, and in the spliceosome contacts U2 proteins and the pre-mRNA, indicating that the U2 snRNP-intron interaction is Prp43's major target.

Indexed as

Gene Expression Regulation, FungalIntronsBinding SitesDEAD-box RNA HelicasesRibonucleoprotein, U2 Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesDEAD-box RNA HelicasesNtr2 protein, S cerevisiaePRP43 protein, S cerevisiaeRibonucleoprotein, U2 Small NuclearSaccharomyces cerevisiae ProteinsSpp382 protein, S cerevisiaebiochemistrychromosomesgeneshelicasesHumanS. cerevisiaespliceosome

Identifiers

PMID27115347
PMCPMC4866824
OpenAlexW2344750900

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Registered trials

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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.