Nup42 FG domain quadrants and their role in Gle1 and Dbp5 interaction

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

The directionality of mRNA transport is enabled by the cytoplasmic enzyme Dbp5 in its removal of Mex67, a protein that binds with mRNA to allow it to exit the nucleus. Dbp5 is assisted by the protein Gle1 to carry out this removal function, and nuclear pore complex (NPC) protein Nup42 is essential for the Gle1-Dbp5 interaction and, consequently, mRNA directionality. The FG domain of Nup42 is required for the Gle1-Dbp5 interaction, but whether only specific sections of the domain are needed is unknown. It is hypothesized that the distal FG domain quadrant is responsible because of needed space between Nup42 and Mex67. This research uses the yeast two-hybrid (Y2H) technique to observe the presence of the Gle1-Dbp5 interaction regarding variable truncations of the FG domain. The current aim is to set up a mutated yeast without Nup42 and with transformed plasmids for Y2H experiment preparation.

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