Date Approved

2019

Degree Type

Open Access Senior Honors Thesis

Department

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.

Included in

Chemistry Commons

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