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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Specific interactions between proteins implicated in splice site selection and regulated alternative splicing

J Y Wu1, T Maniatis

  • 1Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.

Cell
|December 17, 1993
PubMed
Summary

This study reveals that splicing factors SC35 and SF2/ASF bridge 5' and 3' splice sites by interacting with U1 snRNP and U2AF35. These interactions are crucial for pre-mRNA splicing and may regulate alternative splicing via Drosophila Transformer proteins.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Pre-mRNA splicing requires precise recognition and pairing of 5' and 3' splice sites.
  • Splicing factors play critical roles in this intricate molecular process.
  • The U1 small nuclear ribonucleoprotein (snRNP) binds the 5' splice site, and U2AF35-U2AF65 binds the 3' splice site.

Purpose of the Study:

  • To investigate the interaction of splicing factors SC35 and SF2/ASF with components of the spliceosome.
  • To elucidate the role of these interactions in splice site selection and alternative splicing regulation.

Main Methods:

  • Protein-protein interaction assays were used to determine binding partners.
  • The study focused on interactions between SC35, SF2/ASF, U1 snRNP (U1-70K), and U2AF35.

Main Results:

  • SC35 and SF2/ASF were found to specifically interact with both U1-70K and U2AF35.
  • These interactions suggest a bridging function for SR proteins between the 5' and 3' splice sites.
  • Interactions were also observed between SC35, SF2/ASF, U2AF35, and Drosophila splicing regulators Transformer (Tra) and Transformer-2 (Tra2).

Conclusions:

  • SC35 and SF2/ASF act as bridges, connecting the 5' and 3' splice site recognition machinery.
  • Protein-protein interactions mediated by SR proteins are important for splice site selection.
  • These interactions likely play a significant role in the regulation of alternative splicing, as evidenced by interactions with Tra and Tra2.