Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome
| Autor: | Lori A. Kohlstaedt, Andrey Damianov, Douglas L. Black, Donald C. Rio, Shalini Sharma |
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| Rok vydání: | 2008 |
| Předmět: |
Cell Extracts
Spliceosome Biology Heterogeneous ribonucleoprotein particle Models Biological environment and public health Article Cell Line Ribonucleoprotein U1 Small Nuclear Exon Structural Biology RNA Precursors Humans snRNP Polypyrimidine tract-binding protein RNA Processing Post-Transcriptional Molecular Biology Proteins Exons Ribonucleoprotein U2 Small Nuclear Molecular biology Introns Cell biology Polypyrimidine tract RNA splicing Spliceosomes biology.protein Small nuclear ribonucleoprotein Polypyrimidine Tract-Binding Protein Protein Binding |
| Zdroj: | Nature Structural & Molecular Biology. 15:183-191 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsmb.1375 |
| Popis: | The polypyrimidine tract binding protein (PTB) binds pre-mRNAs to alter splice-site choice. We characterized a series of spliceosomal complexes that assemble on a pre-mRNA under conditions of either PTB-mediated splicing repression or its absence. In the absence of repression, exon definition complexes that were assembled downstream of the regulated exon could progress to pre-spliceosomal A complexes and functional spliceosomes. Under PTB-mediated repression, assembly was arrested at an A-like complex that was unable to transition to spliceosomal complexes. Trans-splicing experiments indicated that, even when the U1 and U2 small nuclear ribonucleoprotein particles (snRNPs) are properly bound to the upstream and downstream exons, the presence of PTB prevents the interaction of the two exon complexes. Proteomic analyses of these complexes provide a new description of exon definition complexes, and indicate that splicing regulators can act on the transition between the exon definition complex and an intron-defined spliceosome. |
| Databáze: | OpenAIRE |
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