JMJC Domain-Containing Histone Demethylase 2 (Jhd2): Bridging the Gap between H3K4 Trimethylation and H3 Acetylation

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.

Name thesis:degree_name

Doctor of Philosophy (PhD)

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Year

2014

Author dc:creator

• Harmeyer, Kayla Marie

Contributors dc:contributor

• Scott D Briggs
• Joseph P Ogas
• Ann L Kirchmaier
• Harry Charbonneau

• chromatin
• epigenetics
• H3K14 acetylation
• H3K4 methylation
• histone code
• Jhd2

Repository record dc:identifier

https://docs.lib.purdue.edu/open_access_dissertations/1065

OAI identifier oai:identifier

oai:docs.lib.purdue.edu:open_access_dissertations-2281