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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-9-18
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pubmed:abstractText |
The phosphoprotein P gene of measles virus (Edmonston strain) has been cloned in the Escherichia coli expression vector pET-3a with a histidine tag at the C-terminal end. The expressed protein was soluble, unphosphorylated, and constituted 10 to 20% of total cellular protein. Recombinant P protein purified by Ni-affinity chromatography was found to be efficiently phosphorylated in vitro by recombinant casein kinase II (CKII) or by the CKII activity present in the uninfected cell extract. A comparison of phosphopeptide analyses between the in vivo- and the in vitro-32P-labeled P proteins revealed that both proteins share common phosphorylation sites. In an attempt to identify the exact site of the CKII-mediated phosphorylation, we altered specific serine residues located within the CKII consensus motif to alanine by site-directed mutagenesis. The results indicate that Ser 86, Ser 151, and Ser 180 located within the N-terminal half of the P protein are involved in the CKII-mediated phosphorylation of the P protein.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/P protein, Sendai virus,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
211
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
218-26
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7645214-Alkaloids,
pubmed-meshheading:7645214-Amino Acid Sequence,
pubmed-meshheading:7645214-Animals,
pubmed-meshheading:7645214-Base Sequence,
pubmed-meshheading:7645214-Blotting, Western,
pubmed-meshheading:7645214-Casein Kinase II,
pubmed-meshheading:7645214-Cell Line,
pubmed-meshheading:7645214-Cloning, Molecular,
pubmed-meshheading:7645214-Cricetinae,
pubmed-meshheading:7645214-DNA Primers,
pubmed-meshheading:7645214-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7645214-Escherichia coli,
pubmed-meshheading:7645214-Genes, Viral,
pubmed-meshheading:7645214-Histidine,
pubmed-meshheading:7645214-Kidney,
pubmed-meshheading:7645214-Measles virus,
pubmed-meshheading:7645214-Molecular Sequence Data,
pubmed-meshheading:7645214-Phosphoproteins,
pubmed-meshheading:7645214-Phosphorylation,
pubmed-meshheading:7645214-Polymerase Chain Reaction,
pubmed-meshheading:7645214-Protein Kinase C,
pubmed-meshheading:7645214-Protein-Serine-Threonine Kinases,
pubmed-meshheading:7645214-Recombinant Proteins,
pubmed-meshheading:7645214-Restriction Mapping,
pubmed-meshheading:7645214-Sequence Tagged Sites,
pubmed-meshheading:7645214-Serine,
pubmed-meshheading:7645214-Staurosporine,
pubmed-meshheading:7645214-Viral Proteins
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pubmed:year |
1995
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pubmed:articleTitle |
Involvement of cellular casein kinase II in the phosphorylation of measles virus P protein: identification of phosphorylation sites.
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pubmed:affiliation |
Department of Molecular Biology, Cleveland Clinic Foundation, Ohio 44195, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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