Identifying RNA-Binding Protein Targeted by Dbp5 Through a Multi-copy Suppressor Screening

Publication Date

Spring 2026

Presentation Length

Poster/Gallery presentation

College

College of Sciences & Mathematics

Department

Biology, Department of

Student Level

Undergraduate

Faculty Mentor

Rebecca Adams, PhD

Presentation Type

Poster

Summary

In the nucleus, mRNA transcribed and exported to the cytoplasm for protein translation. This process requires protein remodeling at the nuclear pore complex.  We are looking into whether Dbp5 has additional functions in the nucleus and cytoplasm beyond its known role at the nuclear pore complex (NPC). Nup159 plays a role in anchoring Dbp5 at the nuclear pore, allowing Dbp5 to bind to Mex67, an RNA-binding protein. Once Mex67 is no longer bound to the RNA, the RNA is free to enter the cytoplasm to continue with translation. We hypothesize that either nuclear Dbp5, cytoplasmic Dbp5, or both remove specific RNA-binding proteins from mRNA. To test our hypothesis, we will overexpress plasmids and a genetic screen will be performed to identify the plasmids that result in growth of the Dbp5-Nup159 fusion strain. A plasmid library will be created to be used in a yeast transformation which will test for temperature sensitivity to further isolate the unique plasmid responsible for growth of the fusion. Plasmids that result in growth of the Dbp5-Nup15 fusion may contain genes that have alternative functions in the cell. Identifying these genes could reveal RNA-binding proteins that Dbp5 remodels outside the nuclear pore complex. Future studies could potentially focus on identifying the specific functions these proteins may play on mRNA export in the cell.

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