Evidence map›Paper›PMID 17626844›Full record

ArticleRNA (New York, N.Y.)2007

Functional interactions between Prp8, Prp18, Slu7, and U5 snRNA during the second step of pre-mRNA splicing.

Anna Aronova, Dagmar Bacíková, Luciana B Crotti, David S Horowitz, Beate Schwer

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Control of 3' splice site selection inRNA (New York, N.Y.) · 2025
    Article
  2. Article
  3. Control of 3' splice site selection by the yeast splicing factor Fyv6.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Regulation of DEAH/RHA helicases by G-patch proteins.BioMed research international · 2015
    Review
  16. Article
  17. Article
  18. Article
  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.

Anna AronovaDepartment of Microbiology and Immunology, Weill Cornell Medical College, New York, NY 10021, USA.
Dagmar Bacíková
Luciana B Crotti
David S Horowitz
Beate Schwer
Uniformed Services University of the Health Sciences · USCornell University · US

Funding

STRUCTURE/FUNCTION ANALYSIS OF SPLICEOSOMAL ATPASESR01GM050288 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI SCHWER, BEATE · 1994 to 2011
$3.9M
BIOCHEMISTRY OF PREMRNA SPLICING FACTORSR01GM057267 · NIGMS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI HOROWITZ, DAVID S · 1999 to 2004
$737k
NIGMS NIH HHS GM50288NIGMS NIH HHS GM57267NIGMS NIH HHS R01 GM050288NIGMS NIH HHS R01 GM057267
6 · The paper itself

Abstract

After the second transesterification step of pre-mRNA splicing, the Prp22 helicase catalyzes release of spliced mRNA by disrupting contacts in the spliceosome that likely involve Prp8. Mutations at Arg1753 in Prp8, which suppress helicase-defective prp22 mutants, elicit temperature-sensitive growth phenotypes, indicating that interactions in the spliceosome involving Prp8-R1753 might be broken prematurely at 37 degrees C. Here we report that mutations in loop I of the U5 snRNA or in Prp18 can suppress the temperature-sensitive prp8-R1753 mutants. The same gain-of-function PRP18 alleles can also alleviate the growth phenotypes of multiple slu7-ts mutants, indicating a functional link between Prp8 and the second step splicing factors Prp18 and Slu7. These findings, together with the demonstration that changes at Arg1753 in Prp8 impair step 2 of pre-mRNA splicing in vitro, are consistent with a model in which (1) Arg1753 plays a role in stabilizing U5/exon interactions prior to exon joining and (2) these contacts persist until they are broken by the helicase Prp22.

Indexed as

Cells, CulturedEsterificationExonsHumansNuclear ProteinsRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA, FungalRNA PrecursorsRNA, Small NuclearRNA SplicingRNA Splicing FactorsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsNuclear ProteinsPRP18 protein, S cerevisiaePRP8 protein, S cerevisiaeRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA, FungalRNA PrecursorsRNA, Small NuclearRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSLU7 protein, S cerevisiaeU5 small nuclear RNA

Identifiers

PMID17626844
PMCPMC1950762
OpenAlexW2106422996

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.