Abstract
E1 is the DNA replication origin recognition protein for bovine papillomavirus (BPV), and it carries out enzymatic functions required for initiation of viral DNA replication. Cellular mechanisms likely play a role in regulating BPV DNA replication. We are investigating the role of phosphorylation of E1 on viral replication in vivo and on E1 activity in vitro. Serine 109 is a phosphoacceptor in vivo and is targeted by protein kinase A and protein kinase C in vitro. A viral genome carrying a serine 109 to alanine mutation replicates more efficiently than wild-type in vivo in a transient replication assay. Furthermore, purified mutant protein, while having wild-type levels of ATPase activity, is able to bind more origin-containing DNA than wild-type E1. Phosphorylation therefore appears to play a selective role in modulating a specific E1 function during viral DNA replication.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism*
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Alanine
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Animals
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Binding Sites
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Bovine papillomavirus 1 / genetics
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Bovine papillomavirus 1 / physiology*
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CHO Cells
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Cattle
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Cell Line
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Cricetinae
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DNA Helicases*
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DNA Replication*
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DNA, Viral / biosynthesis*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Genome, Viral
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Glutamic Acid
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Mice
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Mutagenesis
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Phosphorylation
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Replication Origin
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Serine
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Spodoptera / cytology
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Tumor Cells, Cultured
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Viral Proteins / genetics
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Viral Proteins / metabolism*
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Virus Replication*
Substances
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DNA, Viral
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DNA-Binding Proteins
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E1 protein, Bovine papillomavirus
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Recombinant Fusion Proteins
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Viral Proteins
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Glutamic Acid
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Serine
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Adenosine Triphosphatases
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DNA Helicases
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Alanine