Evidence map›Paper›PMID 14610285›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

ATP requirement for Prp5p function is determined by Cus2p and the structure of U2 small nuclear RNA.

Rhonda Perriman, Imre Barta, Gia K Voeltz, John Abelson, Manuel Ares

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

57 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
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  4. Control of 3' splice site selection by the yeast splicing factor Fyv6.bioRxiv : the preprint server for biology · 2024
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  16. Review
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  18. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019
    Review
  19. Article
  20. Article
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 2 institutions in 1 country.

Rhonda PerrimanCenter for Molecular Biology of RNA, Sinsheimer Laboratories, University of California, Santa Cruz, CA 95064, USA.
Imre Barta
Gia K Voeltz
John Abelson
Manuel Ares
California Institute of Technology · USUniversity of California, Santa Cruz · US

Funding

STRUCTURE/FUNCTION OF NUCLEIC ACIDSR01GM032637 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI ABELSON, JOHN N · 1985 to 2004
$3.4M
STRUCTURE AND FUNCTION OF NUCLEIC ACIDSR37GM032637 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI ABELSON, JOHN N · 1987 to 1996
–
NIGMS NIH HHS GM32637NIGMS NIH HHS GM47408NIGMS NIH HHS R01 GM032637
6 · The paper itself

Abstract

Stable addition of U2 small nuclear ribonucleoprotein (snRNP) to form the prespliceosome is the first ATP-dependent step in splicing, and it requires the DEXD/H box ATPase Prp5p. However, prespliceosome formation occurs without ATP in extracts lacking the U2 snRNP protein Cus2p. Here we show that Prp5p is required for the ATP-independent prespliceosome assembly that occurs in the absence of Cus2p. Addition of recombinant Cus2p can restore the ATP dependence of prespliceosome assembly, but only if it is added before Prp5p. Prp5p with an altered ATP-binding domain (Prp5-GNTp) can support growth in vivo, but only in a cus2 deletion strain, mirroring the in vitro results. Other Prp5 ATP-binding domain substitutions are lethal, even in the cus2 deletion strain, but can be suppressed by U2 small nuclear RNA mutations that hyperstabilize U2 stem IIa. We infer that the presence of Cus2p and stem IIa-destabilized forms of U2 small nuclear RNA places high demands on the ATP-driven function of Prp5p. Because Prp5p is not dispensable in vitro even in the absence of ATP, we propose that the core Prp5p function in bringing U2 to the branchpoint is not directly ATP-dependent. The positive role of Cus2p in rescuing mutant U2 can be reconciled with its antagonistic effect on Prp5 function in a model whereby Cus2p first helps Prp5p to activate the U2 snRNP for prespliceosome formation but then is displaced by Prp5p before or during the stabilization of U2 at the branchpoint.

Indexed as

Adenosine TriphosphateBase SequenceBinding SitesDEAD-box RNA HelicasesGenes, FungalModels, BiologicalMolecular Sequence DataMutationNucleic Acid ConformationProtein Structure, TertiaryRecombinant ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA, FungalRNA HelicasesRNA, Small NuclearAdenosine TriphosphateCUS2 protein, S cerevisiaeDEAD-box RNA HelicasesPRP5 protein, S cerevisiaeRecombinant ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA, FungalRNA HelicasesRNA, Small NuclearSaccharomyces cerevisiae ProteinsTrans-ActivatorsU2 small nuclear RNA

Identifiers

PMID14610285
PMCPMC283511
OpenAlexW2164351691

What OpenQuestion holds

Textmetadata
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.