Evidence map›Paper›PMID 7565780›Full record

ArticleMolecular and cellular biology1995

Genetic enhancement of RNA-processing defects by a dominant mutation in B52, the Drosophila gene for an SR protein splicing factor.

X Peng, S M Mount

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

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  16. smg mutants affect the expression of alternatively spliced SR protein mRNAs in Caenorhabditis elegans.Proceedings of the National Academy of Sciences of the United States of America · 1997
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  17. Article
  18. RNA splicing specificity determined by the coordinated action of RNA recognition motifs in SR proteins.Proceedings of the National Academy of Sciences of the United States of America · 1997
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  19. Article
  20. Mutations in the small subunit of the Drosophila U2AF splicing factor cause lethality and developmental defects.Proceedings of the National Academy of Sciences of the United States of America · 1996
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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 2 institutions in 1 country.

X PengDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
S M Mount
Columbia University · USUniversity of Maryland, College Park · US

Funding

NIGMS NIH HHS GM37991
6 · The paper itself

Abstract

SR proteins are essential for pre-mRNA splicing in vitro, act early in the splicing pathway, and can influence alternative splice site choice. Here we describe the isolation of both dominant and loss-of-function alleles of B52, the gene for a Drosophila SR protein. The allele B52ED was identified as a dominant second-site enhancer of white-apricot (wa), a retrotransposon insertion in the second intron of the eye pigmentation gene white with a complex RNA-processing defect. B52ED also exaggerates the mutant phenotype of a distinct white allele carrying a 5' splice site mutation (wDR18), and alters the pattern of sex-specific splicing at doublesex under sensitized conditions, so that the male-specific splice is favored. In addition to being a dominant enhancer of these RNA-processing defects, B52ED is a recessive lethal allele that fails to complement other lethal alleles of B52. Comparison of B52ED with the B52+ allele from which it was derived revealed a single change in a conserved amino acid in the beta 4 strand of the first RNA-binding domain of B52, which suggests that altered RNA binding is responsible for the dominant phenotype. Reversion of the B52ED dominant allele with X rays led to the isolation of a B52 null allele. Together, these results indicate a critical role for the SR protein B52 in pre-mRNA splicing in vivo.

Indexed as

Drosophila ProteinsGenes, InsectNuclear ProteinsPhosphoproteinsRNA SplicingAllelesAmino Acid SequenceAnimalsBase SequenceDNA PrimersDrosophila melanogasterFrameshift MutationGenes, DominantMolecular Sequence DataPoint MutationProteinsB52 protein, DrosophilaDNA PrimersDrosophila ProteinsNuclear ProteinsPhosphoproteinsProteinsRNA-Binding ProteinsRNA Splicing Factors

Identifiers

PMID7565780
PMCPMC230879
OpenAlexW2126052494

What OpenQuestion holds

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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.