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dc.contributor.authorBigby, Christina
dc.date.accessioned2013-02-22T19:16:06Z
dc.date.available2013-02-22T19:16:06Z
dc.date.issued2013-02-22
dc.identifier.urihttp://hdl.handle.net/10464/4199
dc.description.abstractTGA2 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.en_US
dc.publisherBrock Universityen_US
dc.subjectSystemic Acquired Resistanceen_US
dc.titleTGA2 dual activity: N-terminus regulation of reversible DNA binding influenced by NPRI and CK2en_US
dc.typeElectronic Thesis or Dissertationen
dc.degree.nameM.Sc. Biotechnologyen_US
dc.degree.levelMastersen_US
dc.contributor.departmentCentre for Biotechnologyen_US
dc.degree.disciplineFaculty of Mathematics and Scienceen_US
dc.embargo.termsNoneen_US


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