pubmed-article:12004059 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C1335858 | lld:lifeskim |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C1705356 | lld:lifeskim |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C0016395 | lld:lifeskim |
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pubmed-article:12004059 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C1538143 | lld:lifeskim |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C1705361 | lld:lifeskim |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
pubmed-article:12004059 | lifeskim:mentions | umls-concept:C1412239 | lld:lifeskim |
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pubmed-article:12004059 | lifeskim:mentions | umls-concept:C2266866 | lld:lifeskim |
pubmed-article:12004059 | pubmed:issue | 30 | lld:pubmed |
pubmed-article:12004059 | pubmed:dateCreated | 2002-7-22 | lld:pubmed |
pubmed-article:12004059 | pubmed:abstractText | The POZ domain is a protein-protein interaction motif that is found in many transcription factors, which are important for development, oncogenesis, apoptosis, and transcription repression. We cloned the POZ domain transcription factor, FBI-1, that recognizes the cis-element (bp -38 to -22) located just upstream of the core Sp1 binding sites (bp -22 to +22) of the ADH5/FDH minimal promoter (bp -38 to +61) in vitro and in vivo, as revealed by electrophoretic mobility shift assay and chromatin immunoprecipitation assay. The ADH5/FDH minimal promoter is potently repressed by the FBI-1. Glutathione S-transferase fusion protein pull-down showed that the POZ domains of FBI-1, Plzf, and Bcl-6 directly interact with the zinc finger DNA binding domain of Sp1. DNase I footprinting assays showed that the interaction prevents binding of Sp1 to the GC boxes of the ADH5/FDH promoter. Gal4-POZ domain fusions targeted proximal to the GC boxes repress transcription of the Gal4 upstream activator sequence-Sp1-adenovirus major late promoter. Our data suggest that POZ domain represses transcription by interacting with Sp1 zinc fingers and by interfering with the DNA binding activity of Sp1. | lld:pubmed |
pubmed-article:12004059 | pubmed:language | eng | lld:pubmed |
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pubmed-article:12004059 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12004059 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12004059 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12004059 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:12004059 | pubmed:author | pubmed-author:HurMan-WookMW | lld:pubmed |
pubmed-article:12004059 | pubmed:author | pubmed-author:EdenbergHowar... | lld:pubmed |
pubmed-article:12004059 | pubmed:author | pubmed-author:LeeDong-KeeDK | lld:pubmed |
pubmed-article:12004059 | pubmed:author | pubmed-author:SuhDongchulD | lld:pubmed |
pubmed-article:12004059 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12004059 | pubmed:day | 26 | lld:pubmed |
pubmed-article:12004059 | pubmed:volume | 277 | lld:pubmed |
pubmed-article:12004059 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12004059 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12004059 | pubmed:pagination | 26761-8 | lld:pubmed |
pubmed-article:12004059 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:12004059 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12004059 | pubmed:articleTitle | POZ domain transcription factor, FBI-1, represses transcription of ADH5/FDH by interacting with the zinc finger and interfering with DNA binding activity of Sp1. | lld:pubmed |
pubmed-article:12004059 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, BK21 Project for Medical Sciences, Institute of Genetic Sciences, Yonsei University School of Medicine, 134 ShinChon-Dong, SeoDaeMoon-Ku, Seoul 120-752, Korea. | lld:pubmed |
pubmed-article:12004059 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12004059 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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