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A Reporter Based Cellular Assay for Monitoring Splicing Efficiency
Published on: September 15, 2021
Interactome for auxiliary splicing factor U2AF(65) suggests diverse roles
Justin R Prigge1, Sonya V Iverson, Ashley M Siders
1Department of Veterinary Molecular Biology, Montana State University, Molecular Biosciences, 960 Technology Blvd., Bozeman, MT 59718, USA.
Biochimica Et Biophysica Acta
|June 23, 2009
Summary
Researchers identified new U2 small nuclear ribonucleoprotein auxiliary factor (U2AF) interactions with splicing and non-splicing proteins. These findings reveal expanded roles for U2AF(65) in gene expression regulation.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- U2 small nuclear ribonucleoprotein auxiliary factor (U2AF) is crucial for pre-mRNA splicing.
- U2AF comprises U2AF(35) and U2AF(65) subunits, interacting with various splicing factors.
- The full spectrum of U2AF(65) interactions and its non-splicing functions remain incompletely understood.
Purpose of the Study:
- To identify novel mammalian proteins interacting with U2AF(65).
- To characterize the interaction regions between U2AF(65) and its binding partners.
- To explore the potential roles of these interactions in gene regulation.
Main Methods:
- Yeast two-hybrid screening was employed to identify U2AF(65)-interacting proteins.
- Interaction validation was performed using known U2AF(65) partners.
- Mapping of interaction domains within U2AF(65) was conducted.
Main Results:
- Fourteen novel U2AF(65)-interacting proteins were identified.
- Confirmed interactions included U2AF(35) and other known splicing factors.
- New interactions were found with splicing-related proteins (DDX39, SFRS3, SFRS18, SNRPA), zinc finger proteins (ZFP809, ZC3H11A), RBM39, DAXX, and SERBP1.
Conclusions:
- U2AF(65) interacts with a broader range of proteins than previously known.
- These interactions suggest U2AF(65) is involved in pre-mRNA splicing, 3'-end processing, and sub-nuclear localization.
- U2AF(65) plays significant roles in both splicing and non-splicing cellular functions.
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