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The transcription initiation factor TFIID, consisting of the TATA box-binding protein (TBP) and many TBP-associated factors (TAFs), plays a central role in both basal and activated transcription. An intriguing finding is that the 80-residue N-terminal region of Drosophila TAF(II)230 [dTAF(II)230-(2-81)] can bind directly to TBP and inhibit its function. Here, studies with mutated forms of TBP demonstrate that dTAF(II)230-(2-81) binds to the concave surface of TBP, which is important for TATA box binding. Previously, it was reported that a point mutation (L114K) on this concave surface destroys the ability of TBP to bind VP16 and to mediate VP16-dependent activation in vitro, but has no effect on basal transcription. Importantly, the same TBP mutation eliminates TBP binding to dTAF(II)230-(2-81). Consistent with these effects of the L114K mutation, dTAF(II)230-(2-81) and the VP16 activation domain compete for binding to wild-type TBP. These results indicate that transcriptional regulation may involve, in part, competitive interactions between transcriptional activators and TAFs on the TBP surface.

proceedings of the national academy of sciences of the united states of america

<i>Drosophila</i> TAF <sub>II</sub> 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Drosophila TAF II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Drosophila TAF _II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein