Linked Life Data

10357929

Source:http://linkedlifedata.com/resource/pubmed/id/10357929

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1999-7-23
pubmed:abstractText
Sex determination in Drosophila depends upon the post-transcriptional regulatory activities of the Sex-lethal (Sxl) gene. Sxl maintains the female determined state and activates female differentiation pathways by directing the female-specific splicing of Sxl and tra pre-mRNAs. While there is compelling evidence that Sxl proteins regulate splicing by directly binding to target RNAs, previous studies indicate that the two Sxl RNA-binding domains are not in themselves sufficient for biological activity and that an intact N-terminal domain is also critical for splicing function. To further investigate the functions of the Sxl N terminus, we ectopically expressed a chimeric protein consisting of the N-terminal 99 amino acids fused to ss-galactosidase. The Nss-gal fusion protein behaves like a dominant negative, interfering with the Sxl autoregulatory feedback loop and killing females. This dominant negative activity can be attributed to the recruitment of the fusion protein into the large Sxl:Snf splicing complexes that are found in vivo and the consequent disruption of these complexes. In addition to the dominant negative activity, the Nss-gal fusion protein has a novel gain-of-function activity in males: it promotes the female-specific processing of tra pre-mRNAs. This novel activity is discussed in light of the blockage model for the tra splicing regulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0950-1991
pubmed:author
pubmed:issnType
Print
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2841-53
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:10357929-Animals, pubmed-meshheading:10357929-Bacterial Proteins, pubmed-meshheading:10357929-Drosophila, pubmed-meshheading:10357929-Drosophila Proteins, pubmed-meshheading:10357929-Escherichia coli Proteins, pubmed-meshheading:10357929-Female, pubmed-meshheading:10357929-Gene Expression Regulation, Developmental, pubmed-meshheading:10357929-Genes, Dominant, pubmed-meshheading:10357929-Genes, Lethal, pubmed-meshheading:10357929-Insect Proteins, pubmed-meshheading:10357929-Male, pubmed-meshheading:10357929-RNA, Messenger, pubmed-meshheading:10357929-RNA Precursors, pubmed-meshheading:10357929-RNA Processing, Post-Transcriptional, pubmed-meshheading:10357929-RNA Splicing, pubmed-meshheading:10357929-RNA-Binding Proteins, pubmed-meshheading:10357929-Recombinant Fusion Proteins, pubmed-meshheading:10357929-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10357929-Sex Determination Processes, pubmed-meshheading:10357929-Transgenes, pubmed-meshheading:10357929-beta-Galactosidase
pubmed:year
1999
pubmed:articleTitle
The N-terminal domain of Sxl protein disrupts Sxl autoregulation in females and promotes female-specific splicing of tra in males.
pubmed:affiliation
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. gdeshpande@molbio.princeton.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.