Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions.
We provide direct evidence that pre-mRNA splicing alters mRNP protein composition. Using a novel in vitro cross-linking approach, we detected several proteins that associate with mRNA exon-exon junctions only as a consequence of splicing. Immunoprecipitation experiments suggested that these proteins are part of a tight complex around the junction. Two ... were identified as SRm160, a nuclear matrix-associated splicing coactivator, and hPrp8p, a core component of U5 snRNP and spliceosomes. Glycerol gradient fractionation showed that a subset of these proteins remain associated with mRNA after its release from the spliceosome. These results demonstrate that the spliceosome can leave behind signature proteins at exon-exon junctions. Such proteins could influence downstream metabolic events in vivo such as mRNA transport, translation, and nonsense-mediated decay.
Mesh Terms:
Antigens, Nuclear, Base Sequence, Cell Nucleus, Exons, HeLa Cells, Humans, Introns, Molecular Sequence Data, Nuclear Matrix-Associated Proteins, Nuclear Proteins, RNA Precursors, RNA Splicing, RNA, Messenger, RNA-Binding Proteins, Ribonucleoprotein, U5 Small Nuclear, Ribonucleoproteins, Spliceosomes
Antigens, Nuclear, Base Sequence, Cell Nucleus, Exons, HeLa Cells, Humans, Introns, Molecular Sequence Data, Nuclear Matrix-Associated Proteins, Nuclear Proteins, RNA Precursors, RNA Splicing, RNA, Messenger, RNA-Binding Proteins, Ribonucleoprotein, U5 Small Nuclear, Ribonucleoproteins, Spliceosomes
Genes Dev.
Date: May. 01, 2000
PubMed ID: 10809668
View in: Pubmed Google Scholar
Download Curated Data For This Publication
143119
Switch View:
- Interactions 3