Investigating the Role of Dbp5 Residues in Its Interaction with Nab2

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

Export of mRNA from the nucleus to the cytoplasm is an essential cellular process that requires coordinated interactions between nuclear pore proteins and RNA-binding factors. The protein Dbp5 plays a critical role in removing certain RNA-binding proteins, such as Nab2, from mature mRNA in the cytoplasm to provide directionality to transport. However, how these proteins are specifically removed while others remain bound is not fully understood. It has been hypothesized that Dbp5 transiently binds with Nab2 to facilitate its removal from mature mRNA. This study investigates whether mutation of specific residues in Dbp5 will alter its interaction with Nab2. It is hypothesized that mutating residues K443, R463, D467, and E471 will disrupt or weaken the Dbp5-Nab2 interaction. To test this, site-directed mutagenesis was used to generate mutant Dbp5 proteins. These constructs were then introduced into yeast, where interaction with Nab2 will be assessed using a split-Venus assay. Currently, the E471 mutation has been successfully generated, representing an initial step in the experimental process. While interaction has not yet been assessed, future experiments using the split-Venus system will determine whether this mutation impacts Dbp5-Nab2 binding. In addition, site-directed mutagenesis is ongoing to generate mutilations at the other residues, and the split-Venus system will be used there as well. These findings will contribute to a better understanding of the molecular mechanisms underlying mRNA export.

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