Belmont University Research Symposium (BURS)

Yeast Two-Hybrid (Y2H) to Test Dbp5-Gle1 Interaction Dependence on Nup42 FG Domain Length

Publication Date

Spring 3-27-2023


Sciences and Mathematics, College of


Biology, Department of

BURS Faculty Advisor

Dr. Adams

Presentation Type

Poster Presentation


The export of mRNA from its site of production in the nucleus into the cytoplasm is crucial for the translation of the encoded protein. A protein called Mex67 allows for the export of mRNA as it permits travel through the nuclear pore complex (NPC) into the cytoplasm. The removal of Mex67 is needed to ensure correct directionality of the mRNA, and this is done by the protein dimer Dbp5-Gle1 at the cytoplasmic side of the NPC. Previous studies have demonstrated that the Dbp5-Gle1 interaction is dependent on the NPC protein Nup42 with additional evidence suggesting that the amino-terminal FG domain is essential for this interaction. It is unknown how long the repetitive Nup42 FG domain must be in order for Dbp5-Gle1 interaction to occur. The question this study is seeking to answer is, what segments of the Nup42 FG domain are required for Dbp5-Gle1 interaction? In order to answer this, a series of deletions were made from a full-length plasmid that encodes NUP42. These plasmids will then be used in a yeast two-hybrid test between Gle1 and Dbp5 in a nup42 D mutant to determine which plasmids restore the Gle1-Dbp5 interaction.

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