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J. Biol. Chem., Vol. 275, Issue 38, 29847-29856, September 22, 2000
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From the Department of Microbiology and Kaplan Comprehensive Cancer
Center, New York University School of Medicine,
New York, New York 10016
The TATA box-binding protein (TBP) and
TBP-associated factors (TAFIIs) compose the general
transcription factor TFIID. The TAFII subunits mediate
activated transcription by RNA polymerase II by interacting directly
with site-specific transcriptional regulators. TAFIIs also
participate in promoter recognition by contacting core promoter
elements in the context of TFIID. To further dissect the contribution
of individual TAFII subunits to mammalian TFIID function,
we employed a vaccinia virus-based protein expression system to study
protein-protein interactions and complex assembly. We identified the
domains of human (h) TAFII130 required for
TAFII-TAFII interactions and formation of a
complex with hTBP, hTAFII100, and hTAFII250.
Functional analysis of partial TFIID complexes formed in
vivo indicated that hTAFII130 was required for
transcriptional activation by Sp1 in vitro. DNase I
footprinting experiments demonstrated that purified
hTBP/hTAFII250 complex reconstituted with or without
additional TAFIIs was significantly reduced for TATA box
binding (as much as 9-fold) compared with free hTBP. By contrast,
hTAFII130 stabilized binding of hTBP to the TATA box,
whereas hTAFII100 had little effect. Thus, our biochemical analysis supports the notion that TAFIIs possess distinct
functions to regulate the activity of TFIID.
Assembly of Partial TFIID Complexes in Mammalian Cells Reveals
Distinct Activities Associated with Individual TATA Box-binding
Protein-associated Factors*
and
*
This work was supported by National Institutes of Health
Grant GM51314.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Hygiene, Kansai Medical University,
Osaka, Japan.
§
Supported in part by the Irma T. Hirschl Trust. To whom
correspondence should be addressed: Dept. of Microbiology and Kaplan Comprehensive Cancer Center, New York University School of Medicine, 550 First Ave., New York, NY 10016. Tel.: 212-263-8945; Fax:
212-263-8276; E-mail: tanesn01@med.nyu.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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