Evidence map›Paper›PMID 24442613›Full record

ArticleRNA (New York, N.Y.)2014

The DExD/H-box ATPase Prp2p destabilizes and proofreads the catalytic RNA core of the spliceosome.

Alissa M Wlodaver, Jonathan P Staley

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.6field-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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Acta crystallographica. Section D, Structural biology · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Structural toggle in the RNaseH domain of Prp8 helps balance splicing fidelity and catalytic efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Review
  20. 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

2 authors at 1 institution in 1 country.

Alissa M Wlodaver
Jonathan P Staley
University of Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Mechanisms for Rearranging RNA during Pre-mRNA Splicing - Renewal 01R01GM062264 · NIGMS · UNIVERSITY OF CHICAGO · PI STALEY, JONATHAN P · 2001 to 2019
$5.3M
NIGMS NIH HHS GM62264NIGMS NIH HHS R01 GM062264NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

After undergoing massive RNA and protein rearrangements during assembly, the spliceosome undergoes a final, more subtle, ATP-dependent rearrangement that is essential for catalysis. This rearrangement requires the DEAH-box protein Prp2p, an RNA-dependent ATPase. Prp2p has been implicated in destabilizing interactions between the spliceosome and the protein complexes SF3 and RES, but a role for Prp2p in destabilizing RNA-RNA interactions has not been explored. Using directed molecular genetics in budding yeast, we have found that a cold-sensitive prp2 mutation is suppressed not only by mutations in SF3 and RES components but also by a range of mutations that disrupt the spliceosomal catalytic core element U2/U6 helix I, which is implicated in juxtaposing the 5' splice site and branch site and in positioning metal ions for catalysis within the context of a putative catalytic triplex; indeed, mutations in this putative catalytic triplex also suppressed a prp2 mutation. Remarkably, we also found that prp2 mutations rescue lethal mutations in U2/U6 helix I. These data provide evidence that RNA elements that comprise the catalytic core are already formed at the Prp2p stage and that Prp2p destabilizes these elements, directly or indirectly, both to proofread spliceosome activation and to promote reconfiguration of the spliceosome to a fully competent, catalytic conformation.

Indexed as

Catalytic DomainDEAD-box RNA HelicasesMutationNucleic Acid ConformationRNA, CatalyticRNA HelicasesRNA, Small NuclearRNA SplicingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesDEAD-box RNA HelicasesPRP2 protein, S cerevisiaeRNA, CatalyticRNA HelicasesRNA, Small NuclearSaccharomyces cerevisiae ProteinsU2 small nuclear RNAU6 small nuclear RNADExD/H-box ATPasePrp2spliceosome activationspliceosome catalytic coreU2/U6 helix I

Identifiers

PMID24442613
PMCPMC3923124
OpenAlexW2077592602

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.