rdf:type |
|
lifeskim:mentions |
umls-concept:C0016395,
umls-concept:C0040648,
umls-concept:C0040649,
umls-concept:C0080347,
umls-concept:C1148673,
umls-concept:C1335858,
umls-concept:C1412239,
umls-concept:C1511029,
umls-concept:C1538143,
umls-concept:C1705356,
umls-concept:C1705361,
umls-concept:C2266866
|
pubmed:issue |
30
|
pubmed:dateCreated |
2002-7-22
|
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.
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/Sp1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ZBTB7A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Zbtb7a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/formaldehyde dehydrogenase...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
26
|
pubmed:volume |
277
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
26761-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12004059-Aldehyde Oxidoreductases,
pubmed-meshheading:12004059-Amino Acid Sequence,
pubmed-meshheading:12004059-Animals,
pubmed-meshheading:12004059-Cell Nucleus,
pubmed-meshheading:12004059-Chromatin,
pubmed-meshheading:12004059-DNA,
pubmed-meshheading:12004059-DNA-Binding Proteins,
pubmed-meshheading:12004059-Deoxyribonuclease I,
pubmed-meshheading:12004059-Gene Library,
pubmed-meshheading:12004059-HeLa Cells,
pubmed-meshheading:12004059-Humans,
pubmed-meshheading:12004059-Mice,
pubmed-meshheading:12004059-Molecular Sequence Data,
pubmed-meshheading:12004059-Multigene Family,
pubmed-meshheading:12004059-Plasmids,
pubmed-meshheading:12004059-Polymerase Chain Reaction,
pubmed-meshheading:12004059-Precipitin Tests,
pubmed-meshheading:12004059-Promoter Regions, Genetic,
pubmed-meshheading:12004059-Protein Binding,
pubmed-meshheading:12004059-Protein Structure, Tertiary,
pubmed-meshheading:12004059-Sequence Homology, Amino Acid,
pubmed-meshheading:12004059-Sp1 Transcription Factor,
pubmed-meshheading:12004059-Transcription, Genetic,
pubmed-meshheading:12004059-Transcription Factors,
pubmed-meshheading:12004059-Zinc Fingers
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pubmed:year |
2002
|
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.
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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.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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