Proving a Dpb5-Mex67 Bind During mRNA Export

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 transport from the nucleus to the cytoplasm of the cell is an important process that involves many of the same proteins or equivalents in yeast and human cells. A few of these include Mex67, a protein that binds mRNA and carries it across the nuclear pore complex into cytoplasm, and Dbp5, a protein whose function of stripping the Mex67 from the mRNA is known but mechanism of doing so isn’t. After identifying four conserved amino acids from yeast to humans on the surface of Dbp5 with unknown purposes, we hypothesize that these amino acids are actually surface binding sites for a Dbp5/Mex67 attachment that allows Dbp5 to separate mRNA from its carrier protein. To prove this, we are currently attempting to mutate these specific amino acids primarily through PCR mutagenesis to show an inability to bind at these spots would lead to defective mRNA transport and eventual cell death. Because we are currently in the process of making these mutations, we are still in the preprocess of testing this bind and therefore, do not yet have any definitive conclusions. Once these mutations are made and confirmed though, we will reinsert this mutated Dbp5 back into cells which will result in cell death if our hypothesis is correct. This would likely prove the amino acids are binding spots and there is truly a functional attachment between Dbp5 and Mex67, expanding our knowledge on the important process of mRNA transport/export.

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