TFIIA-TAF regulatory interplay: NMR evidence for overlapping binding sites on TBP

Stefan Bagby, Tapas K. Mal, Dingjiang Liu, Elaine Raddatz, Yoshihiro Nakatani, Mitsuhiko Ikura

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


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. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)149-154
Number of pages6
JournalFEBS Letters
Issue number2-3
StatePublished - Feb 25 2000

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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