@article{mbs:/content/journal/jgv/10.1099/vir.0.19702-0, author = "Kaushik, Rajnish and Shaila, M. S.", title = "Cellular casein kinase II-mediated phosphorylation of rinderpest virus P protein is a prerequisite for its role in replication/transcription of the genome", journal= "Journal of General Virology", year = "2004", volume = "85", number = "3", pages = "687-691", doi = "https://doi.org/10.1099/vir.0.19702-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.19702-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "Phosphoprotein P of rinderpest virus (RPV), when expressed in E. coli, is present in the unphosphorylated form. Bacterially expressed P protein was phosphorylated by a eukaryotic cellular extract, and casein kinase II (CK II) was identified as the cellular kinase involved in phosphorylation. In vitro phosphorylation of P-deletion mutants identified the N terminus as a phosphorylation domain. In vivo phosphorylation of single or multiple serine mutants of P protein identified serine residues at 49, 88 and 151 as phospho-acceptor residues. The role of P protein phosphorylation in virus replication/transcription was evaluated using the RPV minigenome system and replication/transcription of a reporter gene in vivo. P protein phosphorylation was shown to be essential for in vivo replication/transcription since phosphorylation-null mutants do not support expression of a reporter gene. Transfection of increased amounts of phosphorylation-null mutant did not support minigenome replication/transcription in vivo.", }