Kaushik, Rajnish and Shaila, MS (2004) Cellular casein kinase II-mediated phosphorylation of rinderpest virus P protein is a prerequisite for its role in replication/transcription of the genome. In: Journal of General Virology, 85 (3). pp. 687-691.
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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.
Item Type: | Journal Article |
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Publication: | Journal of General Virology |
Publisher: | Society for General Microbiology |
Additional Information: | The copyright belongs to Society for General Microbiology |
Department/Centre: | Division of Biological Sciences > Microbiology & Cell Biology |
Date Deposited: | 22 May 2006 |
Last Modified: | 19 Sep 2010 04:26 |
URI: | http://eprints.iisc.ac.in/id/eprint/6792 |
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