Abstract
Specific recognition and pairing of the 5′ and 3′ splice sites are critical steps in pre-mRNA splicing. We report that the splicing factors SC35 and SF2 ASF specifically interact with both the integral U1 small nuclear ribonucleoprotein (snRNP U1-70K0 and with the 35 kd subunit of the splicing factor U2AF (U2AF35). Previous studies indicated that the U1 snRNP binds specifically to the 5′ splice site, while U2AF35-U2AF35 heterodimer binds to the 3′ splice site. Together, these observations suggest that SC35 and other members of the SR family of splicing factors may function in splice site selection by acting as a bridge between components bound to the 5′ and 3′ splice sites. Interestingly, SC35, SF2 ASF, and U2AF35 also interact with the Drosophila splicing regulators Transformer (Tra) and Transformer-2 (Tra2), suggesting that protein-protein interactions mediated by SR proteins may also play an important role in regulating alternative splicing.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1061-1070 |
| Number of pages | 10 |
| Journal | Cell |
| Volume | 75 |
| Issue number | 6 |
| DOIs | |
| State | Published - Dec 17 1993 |
Funding
We would like to thank Jeno Gyuris and Roger Brent for generously providing the HeLa cell cDNA library and reagents for the yeast two-hybrid system; Robin Reed for communicating unpublished results; Jack Keene for Ui-70K cDNA; and Jim Olesen, Mary Lynne Hedley, Ming Tian, and Kristen Lynch for control proteins. We are grateful to Richard Axel, Hubert Amrein, Jim Bruzik, Mary Lynne Hedley, Yi Rao, Tom Schaal. Ming Tian. and Ping Zuofor helpful discussion and critical comments on this manuscript. J. Y. W. is supported by a postdoctoral fellowship from the Leukemia Society of America. This work was supported by a National Institutes of Health grant to T. M.
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology