{"id":{"repo_id":"brock","oai_identifier":"oai:brocku.scholaris.ca:10464/4199"},"canonical_url":"https://search.dev.ndltd.org/etd/brock/oai:brocku.scholaris.ca:10464/4199","repository":{"repo_id":"brock","name":"Brock University","base_url":"https://brocku.scholaris.ca/server/oai/request"},"display":{"title":"TGA2 dual activity: N-terminus regulation of reversible DNA binding influenced by NPRI and CK2","abstract":"TGA2 is a dual-function Systemic Acquired Resistance (SAR) transcription factor involved in the activation and repression of pathogenesis-related (PR) genes. Recent studies have shown that TGA2 is able to switch from a basal repressor to activator, likely, through regulatory control from its N-terminus. The N-terminus has also been shown to affect DNA binding of the TGA2 bZIP domain when phosphorylated by Casein Kinase II (CK2). The mechanisms involved for directing a switch from basal repressor to activator, and the role of kinase activity, have not previously been looked at in detail. This study provides evidence for the involvement of a CK2-like kinase in the switch of TGA2 activity from repressor to activator, by regulating the DNA-binding activity of TGA2 by phosphorylating residues in the N terminus of the protein.","abstract_html":"TGA2 is a dual-function Systemic Acquired Resistance (SAR) transcription factor involved in the activation and repression of pathogenesis-related (PR) genes. Recent studies have shown that TGA2 is able to switch from a basal repressor to activator, likely, through regulatory control from its N-terminus. The N-terminus has also been shown to affect DNA binding of the TGA2 bZIP domain when phosphorylated by Casein Kinase II (CK2). The mechanisms involved for directing a switch from basal repressor to activator, and the role of kinase activity, have not previously been looked at in detail. This study provides evidence for the involvement of a CK2-like kinase in the switch of TGA2 activity from repressor to activator, by regulating the DNA-binding activity of TGA2 by phosphorylating residues in the N terminus of the protein.","abstract_has_math":false,"creators":["Bigby, Christina"],"institution":"Brock University","degree_name":"M.Sc. Biotechnology","degree_level":"Masters","degree_discipline":"Faculty of Mathematics and Science","degree_department":"Centre for Biotechnology","school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013-02-22","date_published":"2013-02-22","updated_at":"2026-07-24T01:23:14Z","subjects":["Systemic Acquired Resistance"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10464/4199","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.department","label":"Department","values":["Centre for Biotechnology"]},{"key":"dc:creator","label":"Author","values":["Bigby, Christina"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2013-02-22T19:16:06Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2013-02-22T19:16:06Z"]},{"key":"dc:date.issued","label":"Date","values":["2013-02-22"]},{"key":"dc:type","label":"Dc Type","values":["Electronic Thesis or Dissertation"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Faculty of Mathematics and Science"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.Sc. Biotechnology"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Brock University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Systemic Acquired Resistance"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10464/4199"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["TGA2 is a dual-function Systemic Acquired Resistance (SAR) transcription factor involved in the activation and repression of pathogenesis-related (PR) genes. Recent studies have shown that TGA2 is able to switch from a basal repressor to activator, likely, through regulatory control from its N-terminus. The N-terminus has also been shown to affect DNA binding of the TGA2 bZIP domain when phosphorylated by Casein Kinase II (CK2). The mechanisms involved for directing a switch from basal repressor to activator, and the role of kinase activity, have not previously been looked at in detail. This study provides evidence for the involvement of a CK2-like kinase in the switch of TGA2 activity from repressor to activator, by regulating the DNA-binding activity of TGA2 by phosphorylating residues in the N terminus of the protein."]},{"key":"dc:title","label":"Title","values":["TGA2 dual activity: N-terminus regulation of reversible DNA binding influenced by NPRI and CK2"]}]}],"canonical_facts":{"dc:contributor.department":["Centre for Biotechnology"],"dc:creator":["Bigby, Christina"],"dc:date.accessioned":["2013-02-22T19:16:06Z"],"dc:date.available":["2013-02-22T19:16:06Z"],"dc:date.issued":["2013-02-22"],"dc:description.abstract":["TGA2 is a dual-function Systemic Acquired Resistance (SAR) transcription factor involved in the activation and repression of pathogenesis-related (PR) genes. Recent studies have shown that TGA2 is able to switch from a basal repressor to activator, likely, through regulatory control from its N-terminus. The N-terminus has also been shown to affect DNA binding of the TGA2 bZIP domain when phosphorylated by Casein Kinase II (CK2). The mechanisms involved for directing a switch from basal repressor to activator, and the role of kinase activity, have not previously been looked at in detail. This study provides evidence for the involvement of a CK2-like kinase in the switch of TGA2 activity from repressor to activator, by regulating the DNA-binding activity of TGA2 by phosphorylating residues in the N terminus of the protein."],"dc:identifier.uri":["http://hdl.handle.net/10464/4199"],"dc:subject":["Systemic Acquired Resistance"],"dc:title":["TGA2 dual activity: N-terminus regulation of reversible DNA binding influenced by NPRI and CK2"],"dc:type":["Electronic Thesis or Dissertation"],"thesis:degree_discipline":["Faculty of Mathematics and Science"],"thesis:degree_level":["Masters"],"thesis:degree_name":["M.Sc. Biotechnology"],"thesis:institution_name":["Brock University"]},"updated_at":"2026-07-24T01:23:14Z"}