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J. Biol. Chem., Vol. 275, Issue 41, 31914-31920, October 13, 2000
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From the Departments of Internal Medicine and Biochemistry, Ryburn
Center for Molecular Cardiology, University of Texas Southwestern
Medical Center, Dallas, Texas 75390-8573
It has been suggested that complexes between
gene-specific activators and the TATA-binding protein (TBP) play an
important role in the expression of many genes. However, few detailed
studies of well defined activator-TBP complexes have been reported. An analysis of the biochemical properties of the complex formed by the
acidic activation domain (AAD) of the yeast activator Gal4 and TBP is
presented here. This is shown to be composed of two AAD and one TBP
molecule. DNA binding experiments reveal that TATA-containing DNAs and
the Gal4 AAD bind TBP competitively, suggesting that the AAD and TATA
boxes recognize overlapping surfaces of TBP. The kinetics of the
formation and dissociation of the AAD2-TBP complex is
also probed. The impact of these findings on models for Gal4-mediated
transcriptional activation is considered.
Biochemical Characterization of the TATA-binding Protein-Gal4
Activation Domain Complex*
,
*
This work was supported in part by American Cancer Society
Grant NP-935 and Welch Foundation Grant I-1299.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.
Partially supported by National Institutes of Health Training
Grant HLO7360.
§
To whom correspondence should be addressed: Dept. of Internal
Medicine and Biochemistry, Ryburn Center for Molecular Cardiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-8573. Tel.: 214-648-1239; Fax: 214-648-1415; E-mail: thomas.kodadek@utsouthwestern.edu.
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