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Permanent link (DOI): https://doi.org/10.7939/R3XH59

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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

Descriptions

Other title
Subject/Keyword
Poxvirus DNA Replication
Single Stranded DNA Binding Protein
Vaccinia Virus
Type of item
Thesis
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
Department of Medical Microbiology and Immunology
Specialization
Virology
Date accepted
2013-05-29T10:06:32Z
Graduation date
2013-11
Degree
Master of Science
Degree level
Master's
Abstract
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.
Language
English
DOI
doi:10.7939/R3XH59
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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