Date Approved

2024

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

Harriet Lindsay, Ph.D.

Abstract

UHRF1 and UHRF2 proteins are multi-domain epigenetic proteins. They share many similarities in sequence and structure. The proteins have specific domains used to bind histone tails and nucleosomes. The purpose of our study is to determine if H4K20me3 is a true binding partner for them. To do so, we measured UHRF1 and UHRF2 protein interactions with histone tail peptides and nucleosomes containing H3unmod, H3K9me3, or H4K40me3. These experiments were conducted using peptide fluorescence polarization (FP) assays and nucleosome pull-downs. Both proteins bound H3K9me3 and H4K20me3 peptides well by FP. However, these proteins did not bind tightly to H4K20me3 and H3unmod nucleosomes. A possible explanation is that the structure of the nucleosome hinders H4K20me3 interactions.

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