Evidence map›Paper›PMID 12458792›Full record

ArticleRNA (New York, N.Y.)2002

A conserved Lsm-interaction motif in Prp24 required for efficient U4/U6 di-snRNP formation.

Stephen D Rader, Christine Guthrie

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

50 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mechanisms of Long Non-Coding RNA in Breast Cancer.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. 7SL RNA in vertebrate red blood cells.RNA (New York, N.Y.) · 2018
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Structure and conformational plasticity of the U6 small nuclear ribonucleoprotein core.Acta crystallographica. Section D, Structural biology · 2017
    Article
  16. Article
  17. Substrate-assisted mechanism of RNP disruption by the spliceosomal Brr2 RNA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

2 authors at 1 institution in 1 country.

Stephen D RaderDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California 94143-0448, USA.
Christine Guthrie
University of California, San Francisco · US

Funding

BIOSYNTHESIS OF RNASR01GM021119 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GUTHRIE, CHRISTINE · 1985 to 2015
$12.9M
MRNA SPLICING FACTOR BRR2F32GM018312 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI RADER, STEPHEN D · 1996 to 1999
–
BIOSYNTHESIS OF RNASR37GM021119 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI GUTHRIE, CHRISTINE · 1990 to 1999
–
NIGMS NIH HHS 5 F32 GM18312NIGMS NIH HHS GM21119
6 · The paper itself

Abstract

The assembly of the U4 and U6 snRNPs into the U4/U6 di-snRNP is necessary for pre-mRNA splicing, and in Saccharomyces cerevisiae requires the splicing factor Prp24. We have identified a family of Prp24 homologs that includes the human protein SART3/p110nrb, which had been identified previously as a surface antigen in several cancers. Sequence conservation among the Prp24 homologs reveals the existence of a fourth previously unidentified RNA recognition motif (RRM) in Prp24, which we demonstrate is necessary for growth of budding yeast at 37 degrees C. The family is also characterized by a highly conserved 12-amino-acid motif at the extreme C terminus. Deletion of this motif in Prp24 causes a cold-sensitive growth phenotype and a decrease in base-paired U4/U6 levels in vivo. The mutant protein also has a reduced association with U6 snRNA in extract, and is unable to interact with the U6 Lsm proteins by two-hybrid assay. In vitro annealing assays demonstrate that deletion of the motif causes a defect in U4/U6 formation by reducing binding of Prp24 to its substrate. We conclude that the conserved C-terminal motif of Prp24 interacts with the Lsm proteins to promote U4/U6 formation.

Indexed as

Suppression, GeneticAmino Acid MotifsAmino Acid SequenceBinding SitesBlotting, NorthernConsensus SequenceDNA PrimersFungal ProteinsHumansMolecular Sequence DataNucleic Acid ConformationPhenotypePolymerase Chain ReactionPrecipitin TestsRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearDNA PrimersFungal ProteinsPrp24 protein, S cerevisiaeRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNA, FungalRNA, Small NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID12458792
PMCPMC1370345
OpenAlexW2140700093

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.