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http://purl.uniprot.org/citations/7828586http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7828586http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7828586http://www.w3.org/2000/01/rdf-schema#comment"The X gene of human hepatitis B virus encodes the polypeptide HBx which transactivates viral and host genes through a variety of cis-acting enhancer elements present in RNA polymerases I, II and III promoters. To better understand the mechanism of X transactivation, we cloned cDNAs of proteins that bind HBx. Here we demonstrate that one of these cDNAs is a full-length cDNA of human RPB5, a subunit shared by RNA polymerases. The HBx transactivation domain and the central region of human RPB5 were necessary for the specific binding of the two proteins as shown by: (i) in vitro assays using deletion mutants of fusion proteins; (ii) in vivo assays which detect associated proteins by co-immunoprecipitation of the non-fused proteins from transfected HepG2 cells. Over-expressed HBx seemed to associate with assembled forms of endogenous human RPB5 in HBx-transfected cells, since the endogenous RPB5 co-immunoprecipitated with HBx. The HBx binding region of human RPB5 by itself stimulated chloramphenicol acetyltransferase activities from several different reporters having X-responsive element(s). Our results support the idea that the interaction of HBx and human RPB5 can facilitate HBx transactivation and that human RPB5 has a domain which can communicate with transcriptional regulators."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1995.tb06984.x"xsd:string
http://purl.uniprot.org/citations/7828586http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1995.tb06984.x"xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Lin Y."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Lin Y."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Murakami S."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Murakami S."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Yi M."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Yi M."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Cheong J.H."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/author"Cheong J.H."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/pages"143-150"xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/pages"143-150"xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/title"Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds human hepatitis B virus X protein and may play a role in X transactivation."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/title"Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds human hepatitis B virus X protein and may play a role in X transactivation."xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/7828586http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/7828586http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7828586
http://purl.uniprot.org/citations/7828586http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7828586