Thesis (Ph.D)--Chemistry and Biochemistry, Georgia Institute of Technology, 2009. / Committee Chair: Loren D. Williams; Committee Member: Donald Doyle; Committee Member: Nicholas V. Hud; Committee Member: Roger Wartell; Committee Member: Stephen Harvey. Part of the SMARTech Electronic Thesis and Dissertation Collection.

Thesis (M.S.)--Rutgers University, 2008. / "Graduate Program in Microbiology and Molecular Genetics." Includes bibliographical references (p. 46-48).

Thesis (M.Phil.)--University of Hong Kong, 2001. / Includes bibliographical references (leaves 133-138). Also available in print.

Thesis (Ph. D.)--University of California, Riverside, 2010. / Includes abstract. Available via ProQuest Digital Dissertations. Title from first page of PDF file (viewed May 18, 2010). Includes bibliographical references. Also issued in print.

Thesis (Ph.D.) - University of Queensland, 2004. / Includes bibliography.

Thesis (Ph. D.)--University of Texas at Austin, 2007. / Vita. Includes bibliographical references.

Thesis (Ph. D.)--University of Texas at Austin, 2007. / Vita. Includes bibliographical references.

Thesis (Ph. D.)--University of Washington, 2007. / Vita. Includes bibliographical references (leaves 69-72).

Typescript. Includes vita and abstract. Bibliography: Includes bibliographical references (leaves 151-160). Description: xiii, 160 leaves : ill. ; 29 cm.

The ligand activated transcription factor Aryl Hydrocarbon Receptor (AHR) forms a DNA binding heterodimer with the Aryl Hydrocarbon Nuclear Translocator (ARNT) in response to planar aromatic hydrocarbons. In addition to AHR and ARNT there are at least three other proteins involved in AHR signaling. These proteins are the co-chaperone p23, Ara-9 and two molecules of Heat Shock Protein-90 (HSP-90). This study documents the production of Ara-9 and C∆418 (an ARNT deletion construct) in a modified thioredoxin fusion system. These proteins were expressed in a system that allowed for removal from the fusion partner via a thrombin recognition site as well as the incorporation of an in vitro phosphorylation site. The proteins were then expressed and column purified from E. coli. Once the proteins were expressed and purified they were cleaved from the thioredoxin fusion partner and radioloabeled. Following optimization of the proteolytic digest and radio-labeling each protein was subject to two methods of functional analysis. C∆418 function was assessed by electrophoretic mobility shift assay (EMSA) and proved to effectively form a DNA binding heterodimer with ARNT. In addition the functionality of C∆418 was assessed by co-precipitation showing that the ThioHis-produced C∆418 was indeed able to dimerize with C∆553 (an AHR deletion construct). The ThioHisproduced Ara-9 was also assessed for functionality by EMSA and showed that it was able to restore AHR/ ARNT/DRE complex formation as effectively as Ara-9 produced in a baculovirus system. In addition the function of ThioHis-Ara-9 was also assessed through Far-Western blotting for its ability to associate with renatured HSP-90. These studies involving C∆418 and Ara-9 show that these proteins can be efficiently produced in a functional manner utilizing an inexpensive bacterial system In addition this study documents the production of a plasmid (pCMV-Ara-9) for transfection into the HepG2 cell line to monitor the effects of increased cellular Ara-9 on AHR.