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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1996-8-1
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pubmed:abstractText |
The EBNA-LP protein encoded by the open reading frame in the leader exons of the Epstein-Barr nuclear antigen messages is essential for efficient immortalization of B lymphocytes. Protein-protein interaction studies using affinity precipitation of proteins from [35S]methionine-labeled cell lysates and bacterially expressed maltose binding protein EBNA-LP fusions were performed. A cellular 68/72-kDa doublet protein was detected. This banding pattern was shown to be identical to that obtained in affinity precipitations with fusions of glutathione-S-transferase and Sp1 (a basal transcription factor). For both EBNA-LP and Sp1 the specific interacting cellular proteins have been identified as heat shock proteins (HSP) 72/73. Affinity precipitation of HSP 72/73 with deletion mutants of EBNA-LP maps the interaction domain on EBNA-LP to exon Y2 which is required for immortalization. Immunoprecipitation of EBNA-LP from EBV-positive lymphoblastoid cell lines coprecipitated the HSP 72/73 proteins, indicating that the interaction occurs in vivo as well as in vitro. The association of HSPs with a widening range of nuclear proteins involved in gene expression and proliferation control now includes Sp1 and EBNA-LP and suggests that there is a central role for molecular chaperones in these processes.
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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/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epstein-Barr Virus Nuclear Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Sp1 Transcription Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
220
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
91-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8659132-Antigens, Viral,
pubmed-meshheading:8659132-Cell Line,
pubmed-meshheading:8659132-DNA-Binding Proteins,
pubmed-meshheading:8659132-Epstein-Barr Virus Nuclear Antigens,
pubmed-meshheading:8659132-HSP70 Heat-Shock Proteins,
pubmed-meshheading:8659132-Herpesvirus 4, Human,
pubmed-meshheading:8659132-Humans,
pubmed-meshheading:8659132-Lymphocytes,
pubmed-meshheading:8659132-Precipitin Tests,
pubmed-meshheading:8659132-Protein Binding,
pubmed-meshheading:8659132-Retinoblastoma Protein,
pubmed-meshheading:8659132-Sp1 Transcription Factor,
pubmed-meshheading:8659132-Tumor Cells, Cultured
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pubmed:year |
1996
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pubmed:articleTitle |
Protein-protein interactions between Epstein-Barr virus nuclear antigen-LP and cellular gene products: binding of 70-kilodalton heat shock proteins.
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pubmed:affiliation |
Department of Infectious Diseases and Microbiology, Graduate School of Public Health, University of Pittsburgh, Pennsylvania 15261, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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