Belmont University Research Symposium (BURS)

Publication Date

2024

College

Sciences and Mathematics, College of

Department

Biology, Department of

BURS Faculty Advisor

Dr. Rebecca Adams

Presentation Type

Poster Presentation

Abstract

Mex67 is a protein that permits mRNA to exit the nucleus to the cytoplasm through nuclear pore complexes (NPC), doorways embedded in the nuclear envelope. Mex67 does so by binding to FG domains of NPC proteins, such as Nup42. This binding allows for Mex67 (and, consequently, mRNA) to weave through the nuclear pore and enter the cytoplasm, where the mRNA can then be translated into a protein. What is not understood is which regions in particular of the FG domain of Nup42 are essential for Mex67 to be able to bind. My hypothesis is that there exists a higher affinity region of the Nup42 FG domain to which Mex67 binds. This hypothesis has been tested by conducting a yeast two-hybrid (Y2H) assay between Mex67 and various truncations of Nup42’s FG domain using the budding yeast S. cerevisiae as a model organism. Plasmids containing a Y2H GAD domain fusion with these Nup42 FG domain truncations were generated and transformed into yeast that contained the Y2H GBD-Mex67 plasmid. The transformed yeast will be plated on selective media in which growth indicates a positive interaction between Nup42-Mex67.

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