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Determination of Oligomeric State and Role of the Acidic C Terminal Tail of Vaccinia Virus I3 Single Stranded DNA Binding Protein Open Access


Other title
Poxvirus DNA Replication
Single Stranded DNA Binding Protein
Vaccinia Virus
Type of item
Degree grantor
University of Alberta
Author or creator
Harrison, Melissa L
Supervisor and department
Evans, David (Medical Microbiology and Immunology)
Examining committee member and department
Shmulevitz, Maya (Medical Microbiology and Immunology)
Hazes, Bart (Medical Microbiology and Immunology)
Glover, Mark (Biochemistry)
Department of Medical Microbiology and Immunology
Date accepted
Graduation date
Master of Science
Degree level
Single-stranded DNA (ssDNA) binding proteins (SSB) play a major role in DNA replication, recombination, and repair, by protecting ssDNA from nuclease attack and removing inhibitory secondary structure. Poxviruses are large double stranded DNA viruses that replicate within the cytoplasm of cells, and must encode their own DNA replication proteins. Previous work has identified the Vaccinia I3 protein as the virally encoded SSB. The structure of I3 has not been solved and the amino acid sequence lacks conservation to other SSB proteins, excepting an acidic C terminus. Our work has shown that I3 can form dimeric and tetrameric complexes. Removal of the C terminus prevents tetramer formation and increases the affinity for ssDNA. We have demonstrated that the C terminus is surface exposed and can compete with ssDNA for SSB binding. The C terminus plays a role in virus infection, as its obstruction decreases the amount of viral DNA replication.
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