title: TFIIA-TAF regulatory interplay: NMR evidence for overlapping binding sites on TBP.
abstract: TATA box binding protein (TBP)-promoter interaction nucleates assembly of the RNA polymerase II transcription initiation complex. Transcription factor IIA (TFIIA) stabilizes the TBP-promoter complex whereas the N-terminal domain of the largest TAF(II) inhibits TBP-promoter interaction. We have mapped the interaction sites on TBP of Drosophila TAF(II)230 and yeast TFIIA (comprising two subunits, TOA1 and TOA2), using nuclear magnetic resonance (NMR), and also report structural evidence that subdomain II of the TAF(II)230 N-terminal inhibitory domain and TFIIA have overlapping binding sites on the convex surface of TBP. Together with previous mutational and biochemical data, our NMR results indicate that subdomain II augments subdomain I-mediated inhibition of TBP function by blocking TBP-TFIIA interaction.
authors.affiliation: Division of Molecular Biology, Ontario Cancer Institute, Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ont., Canada.
authors.forename: S
authors.initials: S
authors.lastname: Bagby
authors.forename: T K
authors.initials: TK
authors.lastname: Mal
authors.forename: D
authors.initials: D
authors.lastname: Liu
authors.forename: E
authors.initials: E
authors.lastname: Raddatz
authors.forename: Y
authors.initials: Y
authors.lastname: Nakatani
authors.forename: M
authors.initials: M
authors.lastname: Ikura
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D004330:Drosophila; D029721:Drosophila Proteins; D051548:Histone Acetyltransferases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D016385:TATA Box; D035381:TATA-Binding Protein Associated Factors; D035181:TATA-Box Binding Protein; D035561:Transcription Factor TFIIA; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism*; D019473:Transcription Factors, TFII / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D010446:Peptide Fragments; D029701:Saccharomyces cerevisiae Proteins; D035381:TATA-Binding Protein Associated Factors; D035181:TATA-Box Binding Protein; C441519:TOA1 protein, S cerevisiae; C441520:TOA2 protein, S cerevisiae; D035561:Transcription Factor TFIIA; D035362:Transcription Factor TFIID; D014157:Transcription Factors; D019473:Transcription Factors, TFII; D051548:Histone Acetyltransferases; C069001:TATA-binding protein associated factor 250 kDa