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

Publication Date

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

mRNA export from the nucleus to the cytoplasm is an essential step in gene expression and is regulated by RNA-binding proteins. In budding yeast, S. cerevisiae, Dbp5 facilitates mRNA export at the nuclear pore complex (NPC) by removing messenger ribonucleoproteins such as Mex67. The fusion of Dbp5-Nup159 to the NPC restricts Dbp5’s ability to perform its functions in both the nucleus and cytoplasm, while also suppressing mRNA export at 37°C. We aim to identify the RNA-binding proteins associated with Dbp5 in the nucleus and cytoplasm during mRNA export. We propose that Dbp5 plays a key role in mRNA export by removing specific RNA-binding proteins. Therefore, hypothesize that overexpressing the targeted RNA-binding protein will suppress the growth defects of the mutant strain, fusion of Dbp5-Nup159, at high temperatures. To test this hypothesis and identify the specific RNA-binding protein, we performed a multicopy suppressor screen using the mutant strain with a 2u library containing 1,500 unique plasmids. The transformation grown on -Leu plates at 25°C and 37°C showed similar colony growth, suggesting there was no suppression of the mutant strain at the higher temperature. The number of colonies grown indicates that the 2u library was not successfully screened, reducing the likelihood of identifying the RNA-binding protein involved. In future directions, it is important to improve the efficiency of the 2u library screen and evaluate the mutant’s temperature sensitivity to better help identify the specific RNA-binding protein associated with Dbp5 in the nucleus and cytoplasm.

This document is currently not available here.

Share

COinS