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Article overview
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Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins | R Singh
; J Valcárcel
; M R Green
; | Date: |
26 May 1995 | Journal: | Science, 268 (5214), 1173-6 | Abstract: | In higher eukaryotes, the polypyrimidine-tract (Py-tract) adjacent to the 3’ splice site is recognized by several proteins, including the essential splicing factor U2AF65, the splicing regulator Sex-lethal (Sxl), and polypyrimidine tract-binding protein (PTB), whose function is unknown. Iterative in vitro genetic selection was used to show that these proteins have distinct sequence preferences. The uridine-rich degenerate sequences selected by U2AF65 are similar to those present in the diverse array of natural metazoan Py-tracts. In contrast, the Sxl-consensus is a highly specific sequence, which can help explain the ability of Sxl to regulate splicing of transformer pre-mRNA and autoregulate splicing of its own pre-mRNA. The PTB-consensus is not a typical Py-tract; it can be found in certain alternatively spliced pre-mRNAs that undergo negative regulation. Here it is shown that PTB can regulate alternative splicing by selectively repressing 3’ splice sites that contain a PTB-binding site. | Source: | PubMed, pmid7761834 | Services: | Forum | Review | Favorites |
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