NDLI: Drosophila TAFII230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Content Provider	PubMed Central
Author	Nishikawa, Jun-ichi Kokubo, Tetsuro Horikoshi, Masami Roeder, Robert g. Nakatani, Yoshihiro
Copyright Year	1997
Abstract	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 TAFII230 [dTAFII230-(2–81)] can bind directly to TBP and inhibit its function. Here, studies with mutated forms of TBP demonstrate that dTAFII230-(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 dTAFII230-(2–81). Consistent with these effects of the L114K mutation, dTAFII230-(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.
Starting Page	85
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	94
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1997-01-07
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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