Date of Award
January 2014
Degree Type
Dissertation
Degree Name
Doctor of Philosophy (PhD)
Department
Biochemistry
First Advisor
Scott D Briggs
Committee Member 1
Scott D Briggs
Committee Member 2
Joseph P Ogas
Committee Member 3
Ann L Kirchmaier
Committee Member 4
Harry Charbonneau
Abstract
Gene expression has been shown to be regulated through epigenetic modifications to the N-terminal tail of histones. Among these modifications is methylation of lysine residues. The enzyme Jhd2 is a histone demethylase that functions to remove H3K4 methylation in S. cerevisiae. Jhd2 is a homologue of the human JARID1 family of histone demethylases, which has four members: JARID1A, B, C and D. JARID1B is of particular interest because it has been shown to be up regulated in 90 percent of primary breast cancers. Furthermore, JARID1A has been shown to be up regulated in gastric cancer. Therefore studying how these H3K4 histone demethylases function will give great insight into how JARID1 family members are missregulated during tumorigenesis and how they can be targeted by inhibitors.
Recommended Citation
Harmeyer, Kayla Marie, "JMJC Domain-Containing Histone Demethylase 2 (Jhd2): Bridging the Gap between H3K4 Trimethylation and H3 Acetylation" (2014). Open Access Dissertations. 1065.
https://docs.lib.purdue.edu/open_access_dissertations/1065