Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator.
The TFIID complex consists of the TATA-binding protein (TBP) and associated factors (TAFs) serving to mediate transcriptional activation by promoter-specific regulators. Here we report the cloning of Drosophila TAFII250 and the assembly of a partial complex containing recombinant TBP, TAFII110 and the C-terminal domain of TAFII250. This triple complex supports Sp1 activation and reveals specific interactions between TAFII250, TBP and TAFII110.
Weinzierl
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Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Dynlacht
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Tjian
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D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000502:physiology*; D004330:Drosophila / Q000235:genetics*; D051548:Histone Acetyltransferases; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000235:genetics*; D011994:Recombinant Proteins; D016329:Sp1 Transcription Factor / Q000502:physiology; D035381:TATA-Binding Protein Associated Factors; D035181:TATA-Box Binding Protein; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000502:physiology*; D015533:Transcriptional Activation
D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D011994:Recombinant Proteins; D016329:Sp1 Transcription Factor; D035381:TATA-Binding Protein Associated Factors; D035181:TATA-Box Binding Protein; D035362:Transcription Factor TFIID; D014157:Transcription Factors; D051548:Histone Acetyltransferases; C069001:TATA-binding protein associated factor 250 kDa