Chironomus Tentans-repressor Splicing Factor Represses Sr Protein Function Locally on Pre-mrna Exons and is Displaced at Correct Splice Sites.
From: Department of Molecular Biology and Functional Genomics, Stockholm University, SE-106 91 Stockholm, Sweden.
Molecular biology of the cell
- Publish Date: Jan 2006
- ISSN: 1059-1524
- Volume: 17
- Issue: 1
- Pages: 32-42
- Medium: Print
- Language: English
- Citation (JAMA): Björk Petra, Wetterberg-Strandh Ingela, Baurén Göran, et al. Chironomus Tentans-repressor Splicing Factor Represses Sr Protein Function Locally on Pre-mrna Exons and is Displaced at Correct Splice Sites.. Mol. Biol. Cell Jan 2006;17:32-42
Abstract
Chironomus tentans-repressor splicing factor (Ct-RSF) represses the activation of splicing by SR proteins in vitro. Ct-RSF colocalizes with the Ser-Arg-rich (SR) protein hrp45 in interchromatin granule clusters and coimmunoprecipitates with hrp45 in nuclear extracts. Ct-RSF and hrp45 can also interact directly in vitro. Ct-RSF and hrp45 are recruited together to transcribing genes and associate with growing pre-mRNAs. Ct-RSF and hrp45 colocalize at a large number of gene loci. Injection of anti-Ct-RSF antibodies into nuclei of living cells blocks association of both Ct-RSF and hrp45 with the growing pre-mRNA, whereas binding of U2 small nuclear ribonucleoprotein particle (snRNP) to the pre-mRNA is unaffected. On the intron-rich Balbiani ring (BR) 3 pre-mRNA, hrp45 as well as U1 and U2 snRNPs bind extensively, whereas relatively little Ct-RSF is present. In contrast, the BR1 and BR2 pre-mRNAs, dominated by exon sequences, bind relatively much Ct-RSF compared with hrp45 and snRNPs. Our data suggest that Ct-RSF represses SR protein function at exons and that the assembly of spliceosomes at authentic splice sites displaces Ct-RSF locally.
Mesh Headings (Keywords): Animals, Cells, Cultured, Chironomidae, Exons, Protein Binding, RNA Precursors, RNA Splice Sites, RNA Splicing, RNA-Binding Proteins, Transcription, Genetic
Check for Full Text / PubMed Unique Identifier (PMID): 16236800
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