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.
","abstract_html":"<p>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.</p>","abstract_has_math":false,"creators":["Harmeyer, Kayla Marie"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Scott D Briggs","Joseph P Ogas","Ann L Kirchmaier","Harry Charbonneau"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-01-01T08:00:00Z","date_published":"2014-01-01T08:00:00Z","updated_at":"2026-07-24T03:54:17Z","subjects":["chromatin","epigenetics","H3K14 acetylation","H3K4 methylation","histone code","Jhd2"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://docs.lib.purdue.edu/open_access_dissertations/1056","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Scott D Briggs","Joseph P Ogas","Ann L Kirchmaier","Harry Charbonneau"]},{"key":"dc:creator","label":"Author","values":["Harmeyer, Kayla Marie"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["chromatin","epigenetics","H3K14 acetylation","H3K4 methylation","histone code","Jhd2"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://docs.lib.purdue.edu/open_access_dissertations/1056"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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.
"]},{"key":"dc:title","label":"Title","values":["JMJC Domain-Containing Histone Demethylase 2 (Jhd2): Bridging the Gap between H3K4 Trimethylation and H3 Acetylation"]}]}],"canonical_facts":{"dc:contributor":["Scott D Briggs","Joseph P Ogas","Ann L Kirchmaier","Harry Charbonneau"],"dc:creator":["Harmeyer, Kayla Marie"],"dc:description.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.
"],"dc:identifier":["https://docs.lib.purdue.edu/open_access_dissertations/1056"],"dc:subject":["chromatin","epigenetics","H3K14 acetylation","H3K4 methylation","histone code","Jhd2"],"dc:title":["JMJC Domain-Containing Histone Demethylase 2 (Jhd2): Bridging the Gap between H3K4 Trimethylation and H3 Acetylation"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T03:54:17Z"}