Source:http://linkedlifedata.com/resource/pubmed/id/10506147
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
41
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pubmed:dateCreated |
1999-11-9
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pubmed:abstractText |
Herpes simplex virus type 1 (HSV-1), the prototype alpha-herpesvirus, causes several prominent diseases. The HSV-1 immediate early (IE) protein IE63 (ICP27) is the only regulatory gene with a homologue in every mammalian and avian herpesvirus sequenced so far. IE63 is a multifunctional protein affecting transcriptional and post-transcriptional processes, and it can shuttle from the nucleus to the cytoplasm. To identify interacting cellular proteins, a HeLa cDNA library was screened in the yeast two-hybrid system using IE63 as bait. Several interacting proteins were identified including heterogeneous nuclear ribonucleoprotein K (hnRNP K), a multifunctional protein like IE63, and the beta subunit of casein kinase 2 (CK2), a protein kinase, and interacting regions were mapped. Confirmation of interactions was provided by fusion protein binding assays, co-immunoprecipitation from infected cells, and CK2 activity assays. hnRNP K co-immunoprecipitated from infected cells with anti-IE63 serum was a more rapidly migrating subfraction than hnRNP K immunoprecipitated by anti-hnRNP K serum. Using anti-IE63 serum, both IE63 and hnRNP K were phosphorylated in vitro by CK2, while in immunoprecipitates using anti-hnRNP K serum, IE63 but not hnRNP K was phosphorylated by CK2. These data provide important new insights into how this key viral regulatory protein exerts its functions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/HNRNPK protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ICP27 protein, human herpesvirus 1,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28991-8
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pubmed:dateRevised |
2010-9-15
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pubmed:meshHeading |
pubmed-meshheading:10506147-Animals,
pubmed-meshheading:10506147-Casein Kinase II,
pubmed-meshheading:10506147-Cell Line,
pubmed-meshheading:10506147-Cricetinae,
pubmed-meshheading:10506147-Gene Expression Regulation, Viral,
pubmed-meshheading:10506147-HeLa Cells,
pubmed-meshheading:10506147-Humans,
pubmed-meshheading:10506147-Immediate-Early Proteins,
pubmed-meshheading:10506147-Phosphorylation,
pubmed-meshheading:10506147-Precipitin Tests,
pubmed-meshheading:10506147-Protein Binding,
pubmed-meshheading:10506147-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10506147-Recombinant Fusion Proteins,
pubmed-meshheading:10506147-Ribonucleoproteins,
pubmed-meshheading:10506147-Yeasts
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pubmed:year |
1999
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pubmed:articleTitle |
The multifunctional herpes simplex virus IE63 protein interacts with heterogeneous ribonucleoprotein K and with casein kinase 2.
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pubmed:affiliation |
Institute of Virology, University of Glasgow, Church St., Glasgow G11 5JR, Scotland, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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