Date of Award
Master of Science
Microbiology and Immunology
Dr. Joe Mymryk
In this study, I show that the HPV16 E7 protein is able to form homodimers in vivo and that the formation of this tertiary structure is primarily dependent on the structural integrity of the CR3 monomer. A collection of E7 mutants targeting residues of the N- terminus, hydrophobic core of the dimer and the solvent exposed residues of CR3 were evaluated for their ability to dimerize in the yeast two-hybrid assay. This new set of mutants was also used to map the interaction between E7 and the pCAF acetyltransferase to the C-terminal region of E7. Binding to pCAF appears to require dimerization of E7 but only one monomer of E7 is involved at any given time. In conclusion, the characterization of these mutants for dimerization and for the interaction with cellular proteins will ultimately pave the way for functional studies to determine the role of dimerization in the HPV life cycle.
Hung, Katherine, "Comprehensive Analysis of Residues in Conserved Region 3 of the HPVI6 E7 protein Involved in Dimerization of E7 and Interaction with pCAF" (2009). Digitized Theses. 3847.