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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1991-9-18
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pubmed:abstractText |
A key step in the regulation of transcription involves interactions between promoter-selective factors and various components of the transcriptional apparatus. Here we report the requirements for transcriptional activation directed by NTF-1, a developmentally regulated transcription factor in Drosophila. Reconstituted transcription with fractionated Drosophila basal factors reveals that activation by NTF-1 requires factors present in the endogenous TFIID fraction that are distinct from the purified TATA-binding protein (TBP). Glycerol gradient sedimentation and immunoprecipitation analyses indicate that TFIID is a multiprotein complex containing TBP and at least six tightly bound TBP-associated factors (TAFs). Preparations of TBP lacking TAFs after fractionation with denaturants no longer support activation by NTF-1 but retain basal level activity. Addition of immunopurified and renatured TAFs to free TBP restores the ability of NTF-1 to activate transcription without influencing basal transcription. These results suggest that one or more of the TAF polypeptides confer coactivator function.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Urea,
http://linkedlifedata.com/resource/pubmed/chemical/grh protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
66
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pubmed:geneSymbol |
zen
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
563-76
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1907890-Animals,
pubmed-meshheading:1907890-Base Sequence,
pubmed-meshheading:1907890-DNA-Binding Proteins,
pubmed-meshheading:1907890-Drosophila Proteins,
pubmed-meshheading:1907890-Drosophila melanogaster,
pubmed-meshheading:1907890-Gene Expression Regulation,
pubmed-meshheading:1907890-Hot Temperature,
pubmed-meshheading:1907890-Macromolecular Substances,
pubmed-meshheading:1907890-Molecular Sequence Data,
pubmed-meshheading:1907890-Multiprotein Complexes,
pubmed-meshheading:1907890-Oligonucleotides,
pubmed-meshheading:1907890-Protein Binding,
pubmed-meshheading:1907890-Recombinant Proteins,
pubmed-meshheading:1907890-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:1907890-Transcription, Genetic,
pubmed-meshheading:1907890-Transcription Factor TFIID,
pubmed-meshheading:1907890-Transcription Factors,
pubmed-meshheading:1907890-Urea
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pubmed:year |
1991
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pubmed:articleTitle |
Isolation of coactivators associated with the TATA-binding protein that mediate transcriptional activation.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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