Evidence map›Paper›PMID 9858581›Full record

ArticleMolecular and cellular biology1999

Elevated levels of a U4/U6.U5 snRNP-associated protein, Spp381p, rescue a mutant defective in spliceosome maturation.

S Lybarger, K Beickman, V Brown, N Dembla-Rajpal, K Morey, R Seipelt, B C Rymond

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Inhibition of a spliceosome turnover pathway suppresses splicing defects.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  12. Review
  13. Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins.Proceedings of the National Academy of Sciences of the United States of America · 1999
    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

7 authors at 3 institutions in 1 country.

S LybargerT. H. Morgan School of Biological Sciences and The Markey Cancer Center, University of Kentucky, Lexington, Kentucky 40506-0225, USA.
K Beickman
V Brown
N Dembla-Rajpal
K Morey
R Seipelt
B C Rymond
Markey Cancer Center · USUniversity of Kentucky · USUniversity of Michigan–Ann Arbor · US

Funding

FUNCTION OF SNRNP PARTICLES IN PREMRNA SPLICINGR01GM042476 · NIGMS · UNIVERSITY OF KENTUCKY · PI RYMOND, BRIAN C. · 1995 to 2007
$1.7M
FUNCTION OF SNRNP PARTICLES IN PRE-MRNA SPLICINGR29GM042476 · NIGMS · UNIVERSITY OF KENTUCKY · PI RYMOND, BRIAN C. · 1989 to 1993
–
NIGMS NIH HHS GM42476NIGMS NIH HHS R01 GM042476
6 · The paper itself

Abstract

U4 snRNA release from the spliceosome occurs through an essential but ill-defined Prp38p-dependent step. Here we report the results of a dosage suppressor screen to identify genes that contribute to PRP38 function. Elevated expression of a previously uncharacterized gene, SPP381, efficiently suppresses the growth and splicing defects of a temperature-sensitive (Ts) mutant prp38-1. This suppression is specific in that enhanced SPP381 expression does not alter the abundance of intronless RNA transcripts or suppress the Ts phenotypes of other prp mutants. Since SPP381 does not suppress a prp38::LEU2 null allele, it is clear that Spp381p assists Prp38p in splicing but does not substitute for it. Yeast SPP381 disruptants are severely growth impaired and accumulate unspliced pre-mRNA. Immune precipitation studies show that, like Prp38p, Spp381p is present in the U4/U6.U5 tri-snRNP particle. Two-hybrid analyses support the view that the carboxyl half of Spp381p directly interacts with the Prp38p protein. A putative PEST proteolysis domain within Spp381p is dispensable for the Spp381p-Prp38p interaction and for prp38-1 suppression but contributes to Spp381p function in splicing. Curiously, in vitro, Spp381p may not be needed for the chemistry of pre-mRNA splicing. Based on the in vivo and in vitro results presented here, we propose that two small acidic proteins without obvious RNA binding domains, Spp381p and Prp38p, act in concert to promote U4/U5.U6 tri-snRNP function in the spliceosome cycle.

Indexed as

MutationRNA SplicingSaccharomyces cerevisiae ProteinsSpliceosomesAmino Acid SequenceFungal ProteinsGene Expression RegulationGenes, FungalMolecular Sequence DataNuclear ProteinsRepressor ProteinsRibonucleoproteins, Small NuclearRNA PrecursorsRNA Splicing FactorsSaccharomyces cerevisiaeFungal ProteinsNuclear ProteinsPRP38 protein, S cerevisiaeRepressor ProteinsRibonucleoproteins, Small NuclearRNA PrecursorsRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSpp381 protein, S cerevisiae(U4-U6.U5)tri-snRNP-specific protein, S cerevisiae

Identifiers

PMID9858581
PMCPMC83915
OpenAlexW2150428003

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.