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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2001-7-20
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pubmed:abstractText |
The DNA-binding domain of nuclear hormone receptors functions as an interaction interface for other transcription factors. Using the DNA-binding domain of TRbeta1 as bait in the yeast two-hybrid system, we cloned the Tat binding protein-1 that was originally isolated as a protein binding to the human immunodeficiency virus type 1 Tat transactivator. Tat binding protein-1 has subsequently been identified as a member of the ATPase family and a component of the 26S proteasome. Tat binding protein-1 interacted with the DNA-binding domain but not with the ligand binding domain of TR in vivo and in vitro. TR bound to the amino-terminal portion of Tat binding protein-1 that contains a leucine zipper-like structure. In mammalian cells, Tat binding protein-1 potentiated the ligand-dependent transactivation by TRbeta1 and TRalpha1 via thyroid hormone response elements. Both the intact DNA-binding domain and activation function-2 of the TR were required for the transcriptional enhancement in the presence of Tat binding protein-1. Tat binding protein-1 did not augment the transactivation function of the RAR, RXR, PPARgamma, or ER. The intrinsic activation domain in Tat binding protein-1 resided within the carboxyl-terminal conserved ATPase domain, and a mutation of a putative ATP binding motif but not a helicase motif in the carboxyl-terminal conserved ATPase domain abolished the activation function. Tat binding protein-1 synergistically activated the TR-mediated transcription with the steroid receptor coactivator 1, p120, and cAMP response element-binding protein, although Tat binding protein-1 did not directly interact with these coactivators in vitro. In contrast, the N-terminal portion of Tat binding protein-1 directly interacted in vitro and in vivo with the TR-interacting protein 1 possessing an ATPase activity that interacts with the activation function-2 of liganded TR. Collectively, Tat binding protein-1 might function as a novel DNA-binding domain-binding transcriptional coactivator specific for the TR probably in cooperation with other activation function-2-interacting cofactors such as TR-interacting protein 1.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Herpes Simplex Virus Protein Vmw65,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/PSMC3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0888-8809
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1329-43
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11463857-Adenosine Triphosphatases,
pubmed-meshheading:11463857-Adenosine Triphosphate,
pubmed-meshheading:11463857-Binding Sites,
pubmed-meshheading:11463857-Cloning, Molecular,
pubmed-meshheading:11463857-DNA,
pubmed-meshheading:11463857-DNA-Binding Proteins,
pubmed-meshheading:11463857-Dimerization,
pubmed-meshheading:11463857-Drug Synergism,
pubmed-meshheading:11463857-Fungal Proteins,
pubmed-meshheading:11463857-Gene Expression,
pubmed-meshheading:11463857-Glutathione Transferase,
pubmed-meshheading:11463857-HIV-1,
pubmed-meshheading:11463857-Herpes Simplex Virus Protein Vmw65,
pubmed-meshheading:11463857-Humans,
pubmed-meshheading:11463857-Luciferases,
pubmed-meshheading:11463857-Proteasome Endopeptidase Complex,
pubmed-meshheading:11463857-Receptors, Thyroid Hormone,
pubmed-meshheading:11463857-Recombinant Fusion Proteins,
pubmed-meshheading:11463857-Response Elements,
pubmed-meshheading:11463857-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11463857-Thyroid Hormones,
pubmed-meshheading:11463857-Trans-Activators,
pubmed-meshheading:11463857-Transcription, Genetic,
pubmed-meshheading:11463857-Transcription Factors,
pubmed-meshheading:11463857-Transcriptional Activation,
pubmed-meshheading:11463857-Transfection
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pubmed:year |
2001
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pubmed:articleTitle |
Human immunodeficiency virus type 1 Tat binding protein-1 is a transcriptional coactivator specific for TR.
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pubmed:affiliation |
First Department of Internal Medicine, Gunma University School of Medicine 3-39-15, Maebashi 371-8511, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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