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Distinct Binding Specificities and Functions of Higher Eukaryotic Polypyrimidine Tract-Binding Proteins
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 U2AF 65 , 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 U2AF 65 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.
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Metadata
- Authors
- Singh, R., Valcárcel, J., & Green, M. R.
- Venue
- Science
- Published
- 1995-05-26
- Volume
- 268
- Issue
- 5214
- Pages
- 1173-1176
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2059293195
- Cited by
- 537
- References
- 0
- FWCI
- 11.13
- Type
- journal article
- Language
- en
- Open access
- closed
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