Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P.
- 15 July 1992
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 89 (14) , 6570-6574
- https://doi.org/10.1073/pnas.89.14.6570
Abstract
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.Keywords
This publication has 16 references indexed in Scilit:
- Cyclic nucleotide-independent protein kinases from rabbit reticulocytes. Purification of casein kinases.Published by Elsevier ,2021
- Gene expression of vesicular stomatitis virus genome RNAVirology, 1992
- Two distinct protein kinase activities in vesicular stomatitis virions phosphorylate the NS transcription factorVirology, 1991
- Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatasesJournal of Biological Chemistry, 1991
- Alteration of specific amino acid residues in the acidic domain I of VSV phosphoprotein (P) converts a GAL4-P(I) hybrid into a transcriptional activator.1991
- Casein kinase I and II--multipotential serine protein kinases: structure, function, and regulation.1991
- NH2-terminal acidic region of the phosphoprotein of vesicular stomatitis virus can be functionally replaced by tubulin.Proceedings of the National Academy of Sciences, 1988
- Inhibition of the Phosphorylation of the Regulatory Non-structural Protein of Vesicular Stomatitis Virus by an Antiviral Xanthate CompoundJournal of General Virology, 1987
- A synthetic peptide substrate specific for casein kinase II.Proceedings of the National Academy of Sciences, 1985
- Multiple phosphorylation of rabbit skeletal muscle glycogen synthase. Evidence for interactions among phosphorylation sites and the resolution of electrophoretically distinct forms of the subunit.Journal of Biological Chemistry, 1983