Mutagenesis of Dbp5-VC to screen for Nab2 association

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 is an important step in eukaryotic gene expression, involving interactions between RNA-binding proteins at the nuclear pore complex (NPC). In Saccharomyces cerevisiae, Mex67 and Nab2 facilitate mRNA export, while Dbp5 removes specific proteins to allow mRNA into the cytoplasm for translation. Dbp5’s ability to selectively remove Mex67 and Nab2, but not other RNA-binding proteins, leads to the question of how Dbp5 selects for these proteins specifically. It is hypothesized that Dbp5 contains specific binding surfaces for Nab2, which allow for Dbp5 to be selective during mRNA export. To test this, a mutant library of Dbp5 was created and used to test if Nab2 is able to bind to randomly mutated Dbp5. To induce mutations, an optimal concentration of manganese was determined to allow for maximized mutagenesis. Gibson Assembly was performed to assemble Dbp5 mutants, but the experiment resulted in a small mutant library with few colonies. Future directions could include creating a larger mutant library of Dbp5 to screen for mutants with disrupted Nab2 binding to better understand Dbp5’s selectivity during mRNA export.

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