Solution Structure of a TBP–TAFII230 Complex Protein Mimicry of the Minor Groove Surface of the TATA Box Unwound by TBP

AbstractGeneral transcription factor TFIID consists of TATA box–binding protein (TBP) and TBP-associated factors (TAFIIs), which together play a central role in both positive and negative regulation of transcription. The N-terminal region of the 230 kDa Drosophila TAFII (dTAFII230) binds directly to TBP and inhibits TBP binding to the TATA box. We report here the solution structure of the complex formed by dTAFII230 N-terminal region (residues 11–77) and TBP. dTAFII23011–77 comprises three α helices and a β hairpin, forming a core that occupies the concave DNA-binding surface of TBP. The TBP-binding surface of dTAFII230 markedly resembles the minor groove surface of the partially unwound TATA box in the TBP–TATA complex. This protein mimicry of the TATA element surface provides the structural basis of the mechanism by which dTAFII230 negatively controls the TATA box–binding activity within the TFIID complex