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• W80901980 abstract "Research Article1 December 1989free access Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A. D.M. Virshup D.M. Virshup Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author M.G. Kauffman M.G. Kauffman Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author T.J. Kelly T.J. Kelly Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author D.M. Virshup D.M. Virshup Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author M.G. Kauffman M.G. Kauffman Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author T.J. Kelly T.J. Kelly Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205. Search for more papers by this author Author Information D.M. Virshup1, M.G. Kauffman1 and T.J. Kelly1 1Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205. The EMBO Journal (1989)8:3891-3898https://doi.org/10.1002/j.1460-2075.1989.tb08568.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We have made use of the cell-free SV40 DNA replication system to identify and characterize cellular proteins required for efficient DNA synthesis. One such protein, replication protein C (RP-C), was shown to be involved with SV40 large T antigen in the early stages of viral DNA replication in vitro. We demonstrate here that RP-C is identical to the catalytic subunit of cellular protein phosphatase 2A (PP2Ac). The purified protein dephosphorylates specific phosphoamino acid residues in T antigen, consistent with the hypothesis that SV40 DNA replication is regulated by modulating the phosphorylation state of the viral initiator protein. We also show that purified RP-C/PP2Ac preferentially stimulates SV40 DNA replication in extracts from early G1 phase cells. This finding suggests that the activity of a cellular factor that influences the net phosphorylation state of T antigen is cell cycle dependent. Previous ArticleNext Article Volume 8Issue 121 December 1989In this issue RelatedDetailsLoading ..." @default.
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• W80901980 title "Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A." @default.
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