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• W2079462454 startingPage "327" @default.
• W2079462454 abstract "The simian virus 40 (SV40) large T antigen is a multifunctional protein involved in SV40 cell transformation and lytic virus infection. Some of its activities are regulated by interaction with cellular proteins and/or by phosphorylation of T antigen by various protein kinases. In this study, we show that immunopurified T antigen from SV40-transformed cells and from baculovirus-infected insect cells is tightly associated with a protein kinase that phosphorylates T antigen in vitro. In the presence of heparin or a peptide resembling a protein kinase CK2 recognition site, the phosphorylation of T antigen by the associated kinase is reduced whereas a p34cdc2-kinase-specific peptide has no influence. In addition, the T-antigen-associated protein kinase can use GTP and ATP as phosphate donors. These properties together with the observation that immunopurified T antigen can be phosphorylated by the addition of protein kinase CK2 suggest that at least one of the T-antigen-associated protein kinases is CK2 or a protein-kinase-CK2-related enzyme. The association of recombinant CK2 with T antigen was strongly confirmed by in vitro binding studies. Experiments with temperature-sensitive SV40-transformed cells provide evidence for a close correlation between cell transformation and phosphorylation of T antigen by the associated protein kinase." @default.
• W2079462454 created "2016-06-24" @default.
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• W2079462454 date "1995-10-01" @default.
• W2079462454 modified "2023-09-23" @default.
• W2079462454 title "A Casein-Kinase-2-Related Protein Kinase is Tightly Associated with the Large T Antigen of Simian Virus 40" @default.
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• W2079462454 doi "https://doi.org/10.1111/j.1432-1033.1995.327_1.x" @default.
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