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Adenovirus Chromatin: The Dynamic Nucleoprotein Complex Throughout InfectionGiberson, Andrea N. 23 August 2013 (has links)
Adenovirus (Ad) is a widely studied DNA virus, but the nucleoprotein structure of the
viral genome in the cell is poorly characterized. Our objective is to study Ad DNA-protein
associations and how these affect the viral life cycle. Most of the viral DNA condensing
protein, protein VII, is lost within a few hours of infection and this loss is independent of
transcription. Cellular histones associate with the viral DNA after removal of protein VII,
with a preferential deposition of H3.3. Micrococcal nuclease accessibility assays at 6 hpi
showed laddering of the viral DNA, suggesting the genome is wrapped in physiologically
spaced nucleosomes. Although viral DNA continues to associate with H3.3 at late times of
infection, the overall level of association with histones is greatly reduced. Knockdown of the
H3.3 chaperone HIRA had no effect on the viral life cycle suggesting that other H3.3
chaperones are involved. Our studies have begun to elucidate the nucleoprotein structure of
Ad DNA in the infected cell nucleus.
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Intracellular trafficking of the hantaviral nucleocapsid protein and its function in modulation of immune signalingOntiveros, Steven J. January 2009 (has links) (PDF)
Thesis (Ph.D.)--University of Alabama at Birmingham, 2009. / Title from PDF title page (viewed on July 16, 2010). Includes bibliographical references.
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A Genetic and Structural Analysis of P22 Lysozyme: A ThesisRennell, Dale 01 February 1988 (has links)
P22 lysozyme, encoded by gene 19, is an essential phage protein responsible for hydrolyzing the bacterial cell wall during lytic infection. P22 lysozyme is related to T4 lysozymein its mode of action, substrate specificities, and in its structure. Gene 19 was located on the phage genome, subcloned, and then sequenced. lysozyme was produced in large quantities and purified for biochemical characterization and for crystallograpic studies. Gene 19consists of 146 codons, and encodes a protein with a molecular weight of 16,117.
Amber mutations were created in gene 19 by in vitro primer-directed mutagenesis. The mutations were crossed by homologous recombination onto the phage genome. The phages bearing the amber mutations in gene 19 were screened for the ability to grow on six different amber suppressor strains. Amino acid substitutions that resulted in nonfunctional or less functional lysozyme were determined. Of 60 possible amino acid substitutions at 11 different sites in P22 lysozyme, 20 are deleterious. The phage bearing amber mutations in gene 19that failed to grow on given suppressor strains were reverted and second site intragenic revertants were obtained. The mutations were sequenced.
A substitution of serine for glutamine at residue 82 is compensated for by changing residue 46 from serine to leucine. This single change enables the phage to form a plaque at 300C but not at 400C. When the triple change asn42->lys; ser46->leu; and ser43->pro is present the lysozyme produced is no longer temperature sensitive. The crystal structure of P22 lysozyme is not yet solved. Assuming that the structures of T4 lysozyme and P22 lysozyme are similar, one can examine the positions of equivalent residues in the T4 lysozyme structure. The spatial arrangement of the residues changed by the secondary site mutations and the original substitution can then be visualized. The mutations discussed above all map far from the original mutation on the T4 three dimensional model.
A substitution of leucine for tyrosine at position 22 is compensated for by the double mutation of arg18->ser and ser23->lys. When the equivalent residues are mapped on the T4 three dimensional model the changes map in close proximity to the original mutation.
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Adenovirus Chromatin: The Dynamic Nucleoprotein Complex Throughout InfectionGiberson, Andrea N. January 2013 (has links)
Adenovirus (Ad) is a widely studied DNA virus, but the nucleoprotein structure of the
viral genome in the cell is poorly characterized. Our objective is to study Ad DNA-protein
associations and how these affect the viral life cycle. Most of the viral DNA condensing
protein, protein VII, is lost within a few hours of infection and this loss is independent of
transcription. Cellular histones associate with the viral DNA after removal of protein VII,
with a preferential deposition of H3.3. Micrococcal nuclease accessibility assays at 6 hpi
showed laddering of the viral DNA, suggesting the genome is wrapped in physiologically
spaced nucleosomes. Although viral DNA continues to associate with H3.3 at late times of
infection, the overall level of association with histones is greatly reduced. Knockdown of the
H3.3 chaperone HIRA had no effect on the viral life cycle suggesting that other H3.3
chaperones are involved. Our studies have begun to elucidate the nucleoprotein structure of
Ad DNA in the infected cell nucleus.
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Regulation of antiviral CD8+ T-cell responses by HCVLukens, John R. January 2008 (has links)
Thesis (Ph. D.)--University of Virginia, 2008. / Title from title page. Includes bibliographical references. Also available online through Digital Dissertations.
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