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The synthesis of modified nucleotide 5'-triphosphates and their enzymatic incorporation into DNABraven, Helen Theresa January 1999 (has links)
No description available.
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Structure and Dynamic Studies of Dpo4Lee, Eunjeong January 2020 (has links)
No description available.
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Dissecting genetic and structural determinants of accurate DNA synthesis by DNA polymerase I /Loh, Ern. January 2006 (has links)
Thesis (Ph. D.)--University of Washington, 2006. / Vita. Includes bibliographical references (leaves 84-92).
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Structure of eukaryotic DNA polymerase epsilon and lesion bypass capability /Sabouri, Nasim, January 2008 (has links)
Diss. (sammanfattning) Umeå : Univ., 2008. / Härtill 4 uppsatser.
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5'-3'-nucleases of Escherichia coli and Haemophilus influenzaeThomson, Duncan Paul January 1996 (has links)
No description available.
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The role of residue Y955 of mitochondrial DNA polymerase [gamma] in nucleotide binding and discriminationEstep, Patricia Ann 14 February 2012 (has links)
The human mitochondrial polymerase (pol γ) is a nuclearly-encoded polymerase that is solely responsible for the faithful replication and repair of the mitochondrial genome. The Y955C mutation in pol γ results in early onset progressive external ophthalmoplegia, premature ovarian failure, and Parkinson’s disease. It is believed that the position of this Y955 residue on the catalytic helix in the polymerase makes it responsible for stabilizing the incoming nucleotide. I have investigated the kinetic effect of the Y955C mutation. Mutation of the tyrosine to a cysteine resulted in a decreased maximum rate of polymerization and increased the dissociation constant for incoming nucleotide. In turn, this decreased catalytic efficiency by 30 to 100-fold. In addition, the polymerase did not incorporate all bases with the same efficiency, it was most efficient when incorporating dGTP opposite a dC, but showed less efficient catalysis when faced with an A:T or T:A base-pair. The polymerase also showed reduced discrimination against misincorporation events. However, when presented with an oxidatively-damaged base, 8-oxo-deoxyguanosine, the polymerase chose to incorporate the base in the correct conformation opposite a dC, discriminating against the mutagenic incorporation of 8-oxo-dGTP opposite a dA. The results presented in this thesis suggest that the severe clinical symptoms of patients with this mutation are at least due in part to the reduced efficiency and discrimination of this polymerase γ mutation. / text
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Vaccinia virus DNA polymerase and ribonucleotide reductase: their role in replication, recombination and drug resistanceGammon, Donald Brad Unknown Date
No description available.
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The detection and quantification of genetically modified E. coli using PCRCornett, Johanne Hazel January 2000 (has links)
No description available.
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Vaccinia virus DNA polymerase and ribonucleotide reductase: their role in replication, recombination and drug resistanceGammon, Donald Brad 06 1900 (has links)
Despite the eradication of smallpox, poxviruses continue to cause human disease around the world. At the core of poxvirus replication is the efficient and accurate synthesis and repair of the viral genome. The viral DNA polymerase is critical for these processes. Acyclic nucleoside phosphonate (ANP) compounds that target the viral polymerase are effective inhibitors of poxvirus replication and pathogenesis. Cidofovir (CDV) is an ANP that inhibits vaccinia virus (VAC) DNA polymerase (E9) DNA synthesis and 3-to-5 exonuclease (proofreading) activities. We determined that point mutations in the DNA polymerase genes of ANP-resistant (ANPR) VAC strains were responsible for CDV resistance and resistance to the related compound, HPMPDAP. Although these resistant strains replicated as well as wild-type VAC in culture, they were highly attenuated in mice. The generation of ANPR VAC strains, in combination with our knowledge of how CDV inhibits E9 activities, allowed us to study the hypothesized role of E9 in catalyzing double-strand break repair through homologous recombination. We provide evidence that VAC uses E9 proofreading activity to catalyze genetic recombination through single-strand annealing reactions (SSA) in infected cells. Both the polarity of end resection of recombinant intermediates and the involvement of polymerase proofreading activity establish these poxviral SSA reactions as unique among homologous recombination schemes. Furthermore, we identified roles for the VAC single-stranded DNA-binding (SSB) protein and nucleotide pools in regulating these reactions. During these later studies we uncovered a differential requirement for the large and small subunits of the VAC ribonucleotide reductase (RR) in viral replication and pathogenesis. Our studies suggest that poxviral RR small subunits form functional complexes with host large RR subunits to provide sufficient nucleotide pools to support DNA replication. We present a model whereby interaction of VAC SSB and RR proteins at replication forks allows for modulation of E9 activity through local nucleotide pool changes, which serves to maximize replication rates while still allowing for recombinational repair. / Virology
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Functional significance of multiple poly(A) polymerases (PAPs) /Nordvarg, Helena, January 2002 (has links)
Diss. (sammanfattning) Uppsala : Univ., 2002. / Härtill 3 uppsatser.
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