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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 |
1997-10-9
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pubmed:abstractText |
The Epstein-Barr virus (EBV) EBNA-1 protein has a central role in the maintenance of a latent EBV infection and is the only virus-encoded protein expressed in all EBV-associated tumors. EBNA-1 is required for replication of the episomal form of the latent viral genome and transactivates the latency C and LMP-1 promoters. The mechanisms by which EBNA-1 performs these functions are not known. Here we describe the cloning, expression, and characterization of a cellular protein, P32/TAP, which strongly interacts with EBNA-1. We show that P32/TAP is expressed at high levels in Raji cells and is synthesized as a proprotein of 282 amino acids (aa) that is posttranslationally processed by a two-step cleavage process to yield a mature protein of 209 aa. It has been previously reported that P32/TAP is expressed on the cell surface. Our transient expression assays detected full-length P32/TAP (1-282 aa) in the cytoplasm while mature P32/TAP protein localized to the nucleus. Three lines of evidence support P32/TAP interaction with EBNA-1. First, in the yeast two-hybrid system we mapped two interactive N-terminal regions of EBNA-1, aa 40-60 and aa 325-376, each of which contains arginine-glycine repeats. These regions interact with the C-terminal half of P32/TAP. Second, the full-length cytoplasmic P32/TAP protein can translocate nuclear EBNA-1 into the cytoplasm. Third, P32/TAP co-immunoprecipitated with EBNA-1. We have confirmed that a Gal4 fusion protein containing the C-terminal region of P32/TAP (aa 244-282) transactivates expression from a reporter containing upstream Gal4-binding sites. Deletion of the P32/TAP interactive regions of EBNA-1 severely diminished EBNA-1 transactivation of FRTKCAT in transient expression assays. Our data suggest that interaction with P32/TAP may contribute to EBNA-1-mediated transactivation.
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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/Antigens, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/C1QBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/C1qbp protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Epstein-Barr Virus Nuclear Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/complement 1q receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1997 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
236
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18-29
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9299613-Amino Acid Sequence,
pubmed-meshheading:9299613-Animals,
pubmed-meshheading:9299613-Antigens, CD44,
pubmed-meshheading:9299613-Arginine,
pubmed-meshheading:9299613-Binding Sites,
pubmed-meshheading:9299613-Carrier Proteins,
pubmed-meshheading:9299613-Cell Line,
pubmed-meshheading:9299613-Cercopithecus aethiops,
pubmed-meshheading:9299613-Chloramphenicol O-Acetyltransferase,
pubmed-meshheading:9299613-Cloning, Molecular,
pubmed-meshheading:9299613-Consensus Sequence,
pubmed-meshheading:9299613-DNA, Complementary,
pubmed-meshheading:9299613-DNA Primers,
pubmed-meshheading:9299613-Epstein-Barr Virus Nuclear Antigens,
pubmed-meshheading:9299613-Gene Library,
pubmed-meshheading:9299613-Genome, Viral,
pubmed-meshheading:9299613-Glycine,
pubmed-meshheading:9299613-Herpesvirus 4, Human,
pubmed-meshheading:9299613-Humans,
pubmed-meshheading:9299613-Lymphocytes,
pubmed-meshheading:9299613-Membrane Glycoproteins,
pubmed-meshheading:9299613-Mice,
pubmed-meshheading:9299613-Mitochondrial Proteins,
pubmed-meshheading:9299613-Molecular Sequence Data,
pubmed-meshheading:9299613-Polymerase Chain Reaction,
pubmed-meshheading:9299613-Receptors, Complement,
pubmed-meshheading:9299613-Recombinant Fusion Proteins,
pubmed-meshheading:9299613-Saccharomyces cerevisiae,
pubmed-meshheading:9299613-Sequence Alignment,
pubmed-meshheading:9299613-Transfection
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pubmed:year |
1997
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pubmed:articleTitle |
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
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pubmed:affiliation |
Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, Maryland 21205-2185, 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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