Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P.
We have previously shown that phosphorylation of vesicular stomatitis virus (VSV) phosphoprotein P by cellular protein kinase activity is an essential prerequisite for its transcriptional function. We have now purified this protein kinase by monitoring its ability to phosphorylate bacterially expressed, unphosphorylated P protein. Biochemical studies showed that the kinase is indistinguishable from casein kinase II, a ubiquitous cyclic AMP-independent protein kinase present in a wide variety of eukaryotic cells and tissues. Functional VSV transcription could be reconstituted with viral L protein, N-RNA template, and P protein phosphorylated by either purified cellular protein kinase or purified casein kinase II. The unusual role of casein kinase II in the transcription process of a nonsegmented negative-strand RNA virus would have important implications in host-virus interactions and antiviral therapy.
Barik
S
S
Department of Molecular Biology, Cleveland Clinic Foundation, OH 44195-5069.
Banerjee
A K
AK
D002213:Capsid / Q000378:metabolism*; D047390:Casein Kinase II; D015967:Gene Expression Regulation, Viral; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D012324:RNA-Dependent RNA Polymerase / Q000378:metabolism*; D013379:Substrate Specificity; D014158:Transcription, Genetic; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics*; D014758:Viral Core Proteins / Q000378:metabolism*; D017361:Viral Nonstructural Proteins
D010750:Phosphoproteins; D014758:Viral Core Proteins; D017361:Viral Nonstructural Proteins; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D012324:RNA-Dependent RNA Polymerase