Document Detail


Cellular casein kinase II-mediated phosphorylation of rinderpest virus P protein is a prerequisite for its role in replication/transcription of the genome.
MedLine Citation:
PMID:  14993654     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Rajnish Kaushik; M S Shaila
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of general virology     Volume:  85     ISSN:  0022-1317     ISO Abbreviation:  J. Gen. Virol.     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-02     Completed Date:  2004-04-30     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0077340     Medline TA:  J Gen Virol     Country:  England    
Other Details:
Languages:  eng     Pagination:  687-91     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Casein Kinase II
Cercopithecus aethiops
DNA Replication / genetics
Genes, Reporter
Genome, Viral*
Phosphorylation
Protein-Serine-Threonine Kinases / metabolism*
RNA Replicase / metabolism*
Rinderpest virus / genetics*,  metabolism
Substrate Specificity
Transcription, Genetic / genetics
Vero Cells
Viral Proteins / metabolism*
Chemical
Reg. No./Substance:
0/Viral Proteins; EC 2.7.11.1/Casein Kinase II; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.7.48/RNA Replicase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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