TAF(II)170 interacts with the concave surface of TATA-binding protein to inhibit its DNA binding activity.
The human RNA polymerase II transcription factor B- TFIID consists of TATA- binding protein (TBP) and the TBP-associated factor ( TAF) TAF(II)170 and can rapidly redistribute over promoter DNA. Here we report the identification of human TBP- binding regions in human TAF(II)170. We have defined the TBP interaction domain of TAF(II)170 within three amino-terminal regions: residues 2 to 137, 290 to 381, and 380 to 460. Each region contains a pair of Huntington-elongation-A subunit-Tor repeats and exhibits species-specific interactions with TBP family members. Remarkably, the altered-specificity TBP mutant (TBP(AS)) containing a triple mutation in the concave surface is defective for binding the TAF(II)170 amino-terminal region of residues 1 to 504. Furthermore, within this region the TAF(II)170 residues 290 to 381 can inhibit the interaction between Drosophila TAF(II)230 (residues 2 to 81) and TBP through competition for the concave surface of TBP. Biochemical analyses of TBP binding to the TATA box indicated that TAF(II)170 region 290-381 inhibits TBP-DNA complex formation. Importantly, the TBP(AS) mutant is less sensitive to TAF(II)170 inhibition. Collectively, our results support a mechanism in which TAF(II)170 induces high-mobility DNA binding by TBP through reversible interactions with its concave DNA binding surface.[1]References
- TAF(II)170 interacts with the concave surface of TATA-binding protein to inhibit its DNA binding activity. Pereira, L.A., van der Knaap, J.A., van den Boom, V., van den Heuvel, F.A., Timmers, H.T. Mol. Cell. Biol. (2001) [Pubmed]
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