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Casein kinase II is the P protein phosphorylating cellular kinase associated with the ribonucleoprotein complex of purified vesicular stomatitis virus

Department of Molecular Biology, Research Institute, The Cleveland Clinic Foundation, 9500 Euclid Avenue, NC20, Cleveland, OH 44195, USA

Protein kinase activities associated with a highly purified transcriptionally active ribonucleoprotein complex from the virions of vesicular stomatitis virus (VSV) were isolated and characterized. Based upon several biochemical and immunological criteria, the protein kinase activity, which phosphorylated the bacterially expressed unphosphorylated (P_o) protein, was shown to be cellular casein kinase II (CKII). These studies included inhibition of the protein kinase by specific inhibitors, phosphorylation of mutant phosphoproteins (P), immunoprecipitation by CKII antibody and Western blot analyses, and finally its ability to activate P_o to synthesize RNA in a transcription-reconstitution reaction. The P protein is phosphorylated intracellularly by cellular CKII. The present study demonstrates that VSV specifically packages CKII which remains strongly associated with the ribonucleoprotein complex during morphogenesis.

^* Author for correspondence. Fax +1 216 444 0512. e-mail banerja@ccsmtp.ccf.org

Received 4 August 1994; accepted 28 September 1994.

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