Evidence map›Paper›PMID 24231520›Full record

ArticleRNA (New York, N.Y.)2014

An unanticipated early function of DEAD-box ATPase Prp28 during commitment to splicing is modulated by U5 snRNP protein Prp8.

Argenta M Price, Janina Görnemann, Christine Guthrie, David A Brow

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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 21% 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, 20 citations in OpenAlex.

  1. SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  17. 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

4 authors at 2 institutions in 2 countries.

Argenta M Price
Janina Görnemann
Christine Guthrie
David A Brow
University of California, San Francisco · USUniversity of Wisconsin–Madison · US

Funding

BIOSYNTHESIS OF RNASR01GM021119 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GUTHRIE, CHRISTINE · 1985 to 2015
$12.9M
Structure and Function of U6 Spliceosomal RNAR01GM065166 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BROW, DAVID A, BUTCHER, SAMUEL E · 2002 to 2016
$3.5M
RNA DYNAMICS IN THE SPLICEOSOMER01GM054018 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BROW, DAVID A · 1997 to 2006
$1.1M
NIGMS NIH HHS R01 GM021119NIGMS NIH HHS R01 GM054018NIGMS NIH HHS R01 GM065166
6 · The paper itself

Abstract

The stepwise assembly of the highly dynamic spliceosome is guided by RNA-dependent ATPases of the DEAD-box family, whose regulation is poorly understood. In the canonical assembly model, the U4/U6.U5 triple snRNP binds only after joining of the U1 and, subsequently, U2 snRNPs to the intron-containing pre-mRNA. Catalytic activation requires the exchange of U6 for U1 snRNA at the 5' splice site, which is promoted by the DEAD-box protein Prp28. Because Prp8, an integral U5 snRNP protein, is thought to be a central regulator of DEAD-box proteins, we conducted a targeted search in Prp8 for cold-insensitive suppressors of a cold-sensitive Prp28 mutant, prp28-1. We identified a cluster of suppressor mutations in an N-terminal bromodomain-like sequence of Prp8. To identify the precise defect in prp28-1 strains that is suppressed by the Prp8 alleles, we analyzed spliceosome assembly in vivo and in vitro. Surprisingly, in the prp28-1 strain, we observed a block not only to spliceosome activation but also to one of the earliest steps of assembly, formation of the ATP-independent commitment complex 2 (CC2). The Prp8 suppressor partially corrected both the early assembly and later activation defects of prp28-1, supporting a role for this U5 snRNP protein in both the ATP-independent and ATP-dependent functions of Prp28. We conclude that the U5 snRNP has a role in the earliest events of assembly, prior to its stable incorporation into the spliceosome.

Indexed as

Adenosine TriphosphateAlternative SplicingAmino Acid SequenceAmino Acid SubstitutionDEAD-box RNA HelicasesModels, MolecularMolecular Sequence DataProtein MultimerizationRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA, Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSpliceosomesAdenosine TriphosphateDEAD-box RNA HelicasesPRP28 protein, S cerevisiaePRP8 protein, S cerevisiaeRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA, Small NuclearSaccharomyces cerevisiae ProteinsU5 small nuclear RNAcommitment complexpre-mRNA splicingpre-spliceosomePrp28Prp8

Identifiers

PMID24231520
PMCPMC3866644
OpenAlexW2138260766

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.