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rdf:type |
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lifeskim:mentions |
umls-concept:C0019169,
umls-concept:C0032214,
umls-concept:C0035681,
umls-concept:C0035700,
umls-concept:C0035820,
umls-concept:C0040624,
umls-concept:C0062529,
umls-concept:C0086418,
umls-concept:C1145667,
umls-concept:C1418743,
umls-concept:C1522138,
umls-concept:C1711351
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pubmed:issue |
1
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pubmed:dateCreated |
1995-2-17
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1309924,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1360668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1484484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1549357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1638635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1653503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1827531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1856209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-1883205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2034275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2125986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2154703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2186966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2227262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2303039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2323335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2359621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2538828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2548156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2744487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2753903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2822953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-2995835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-3186723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-3670292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-3855246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8116251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8133894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8195148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8248780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8249276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8367466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8390762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8437213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8441471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7828586-8502480
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
143-50
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7828586-Amino Acid Sequence,
pubmed-meshheading:7828586-Blotting, Western,
pubmed-meshheading:7828586-Cells, Cultured,
pubmed-meshheading:7828586-Cloning, Molecular,
pubmed-meshheading:7828586-DNA-Directed RNA Polymerases,
pubmed-meshheading:7828586-Eukaryotic Cells,
pubmed-meshheading:7828586-Genes, Reporter,
pubmed-meshheading:7828586-Humans,
pubmed-meshheading:7828586-Liver,
pubmed-meshheading:7828586-Molecular Sequence Data,
pubmed-meshheading:7828586-Nuclear Proteins,
pubmed-meshheading:7828586-Precipitin Tests,
pubmed-meshheading:7828586-Protein Binding,
pubmed-meshheading:7828586-Protein Conformation,
pubmed-meshheading:7828586-Trans-Activators,
pubmed-meshheading:7828586-Transcriptional Activation,
pubmed-meshheading:7828586-Transfection
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pubmed:year |
1995
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pubmed:articleTitle |
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.
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pubmed:affiliation |
Department of Molecular Biology, Kanazawa University, Japan.
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pubmed:publicationType |
Journal Article
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