Testing Nup42 FG Domain Constructs Required for Mex67 Interaction Using a Yeast Two Hybrid Assay

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

In Eukaryotic cells, messenger RNA (mRNA) must be exported from the nucleus to the cytoplasm so it can be translated into proteins. This process happens in the nuclear pore complex (NPC), which controls what molecules can travel between the nucleus and the cytoplasm. The export protein Mex67 helps move mRNA across the NPC through interactions with phenylalanine-glycine (FG) domains found in nucleoporins, like Nup42.

The goal of this project is to determine if there are different regions of the Nup42 FG domain that are required for interaction with Mex67. I hypothesize that only certain segments of the FG domain will support binding while other sections will not be sufficient.

To test this, varying segments of the Nup42 FG domain were expressed in a yeast two hybrid assay with Mex67, and interaction was determined by growth on a histidine deficient media.

The results show that some FG domain segments allow for interaction with Mex67, while others do not. This indicates that there is a specific area in the FG domain required for binding. A possibility for future work includes identifying the smallest region required for interaction and how this might relate to other proteins involved in mRNA export.

This document is currently not available here.

Share

COinS