Casein kinase II is the P protein phosphorylating cellular kinase associated with the ribonucleoprotein complex of purified vesicular stomatitis virus.
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 (Po) 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 Po 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.
Department of Molecular Biology, Cleveland Clinic Foundation, OH 44195.
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Gupta
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Das
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Banerjee
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D047390:Casein Kinase II; D002478:Cells, Cultured; D006224:Cricetinae; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000302:isolation & purification* / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism*; D014158:Transcription, Genetic; D014721:Vesicular stomatitis Indiana virus / Q000201:enzymology*; D014764:Viral Proteins / Q000378:metabolism*
D010750:Phosphoproteins; D012261:Ribonucleoproteins; D014764:Viral Proteins; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases