Evidence map›Paper›PMID 15542821›Full record

ArticleMolecular and cellular biology2004

Interaction between a G-patch protein and a spliceosomal DEXD/H-box ATPase that is critical for splicing.

Edward J Silverman, Ayaka Maeda, Janet Wei, Paul Smith, Jean D Beggs, Ren-Jang Lin

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
1.6field-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

72 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. 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
    Article
  9. Article
  10. Article
  11. The structure of Prp2 bound to RNA and ADP-BeFActa crystallographica. Section D, Structural biology · 2021
    Article
  12. DEAH-Box RNA Helicases in Pre-mRNA Splicing.Trends in biochemical sciences · 2021
    Review
  13. Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Acta crystallographica. Section D, Structural biology · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Edward J SilvermanCity of Hope Graduate School of Biological Sciences, Duarte, CA 91010, USA.
Ayaka Maeda
Janet Wei
Paul Smith
Jean D Beggs
Ren-Jang Lin
City Of Hope National Medical Center · USWellcome Centre for Cell Biology · GB

Funding

FUNCTIONAL SPLICEOSOMES AND EXTRINSIC SPLICING FACTORSR01GM040639 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LIN, REN-JANG · 1988 to 2006
$2.0M
NIGMS NIH HHS GM40639NIGMS NIH HHS R01 GM040639
6 · The paper itself

Abstract

Prp2 is an RNA-dependent ATPase that activates the spliceosome before the first transesterification reaction of pre-mRNA splicing. Prp2 has extensive homology throughout the helicase domain characteristic of DEXD/H-box helicases and a conserved carboxyl-terminal domain also found in the spliceosomal helicases Prp16, Prp22, and Prp43. Despite the extensive homology shared by these helicases, each has a distinct, sequential role in splicing; thus, uncovering the determinants of specificity becomes crucial to the understanding of Prp2 and the other DEAH-splicing helicases. Mutations in an 11-mer near the C-terminal end of Prp2 eliminate its spliceosome binding and splicing activity. Here we show that a helicase-associated protein interacts with this domain and that this interaction contributes to the splicing process. First, a genome-wide yeast two-hybrid screen using Prp2 as bait identified Spp2, which contained a motif with glycine residues found in a number of RNA binding proteins. SPP2 was originally isolated as a genetic suppressor of a prp2 mutant. In a reciprocal screen, Spp2 specifically pulled out the C-terminal half of Prp2. Mutations in the Prp2 C-terminal 11-mer that disrupted function or spliceosome binding also disrupted Spp2 interaction. A screen of randomly mutagenized SPP2 clones identified an Spp2 protein with a mutation in the G patch that could restore interaction with Prp2 and enhanced splicing in a prp2 mutant strain. The study identifies a potential mechanism for Prp2 specificity mediated through a unique interaction with Spp2 and elucidates a role for a helicase-associated protein in the binding of a DEXD/H-box protein to the spliceosome.

Indexed as

RNA SplicingAdenosine TriphosphatasesAllelesAlternative SplicingAmino Acid MotifsAmino Acid Sequencebeta-GalactosidaseBlotting, WesternDEAD-box RNA HelicasesGenes, ReporterGenetic VectorsGlutathione TransferaseGlycineHistidineMolecular Sequence DataMutationAdenosine Triphosphatasesbeta-GalactosidaseDEAD-box RNA HelicasesGlutathione TransferaseGlycineHistidinePRP2 protein, S cerevisiaeRNASaccharomyces cerevisiae ProteinsSPP2 protein, S cerevisiae

Identifiers

PMID15542821
PMCPMC529041
OpenAlexW2107344403

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.