Date Approved
2019
Degree Type
Open Access Senior Honors Thesis
Department or School
Chemistry
First Advisor
Brittany Albaugh, Ph.D.
Second Advisor
Hedeel Evans, Ph.D.
Third Advisor
Deborah Heyl-Clegg, Ph.D.
Abstract
Every cell contains the same genetic code, to have cell differentiation this genetic code needs to be regulated on what is expressed. The regulation of gene expression without altering the genetic code itself is known as epigenetics. An example of epigenetic regulation can be seen between the binding of UHRF2 and H3 histones. The purpose of this project is to determine ifD363 in UHRF2 is important for histone H3 binding. To do so, D363 was mutated to alanine, lysine or asparagine. The mutant protein was expressed, purified, and its ability to binding to H3 was tested by fluorescence polarization. Compared to wildtype UHRF2 PHD which bound histone H3, the D363A, D363K and D363N mutants showed no binding. This suggests D363 is critical for the UHRF2: H3 interaction.
Recommended Citation
Gilliam, Marisa, "Characterization of the histone binding properties of the epigenetic reader protein UHRF2 to H3 in PHD domain" (2019). Senior Honors Theses and Projects. 645.
https://commons.emich.edu/honors/645