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  • Title: Modulation of bovine papillomavirus DNA replication by phosphorylation of the viral E1 protein.
    Author: Zanardi TA, Stanley CM, Saville BM, Spacek SM, Lentz MR.
    Journal: Virology; 1997 Feb 03; 228(1):1-10. PubMed ID: 9024804.
    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.
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