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Originally published In Press as doi:10.1074/jbc.M109246200 on October 24, 2001

J. Biol. Chem., Vol. 276, Issue 52, 49100-49109, December 28, 2001
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Fluorescence-based Analyses of the Effects of Full-length Recombinant TAF130p on the Interaction of TATA Box-binding Protein with TATA Box DNA*

Utpal Banik, Joseph M. BeechemDagger , Edward Klebanow§, Stephanie Schroeder, and P. Anthony Weil||

From the Department of Molecular Physiology and Biophysics, Vanderbilt University, School of Medicine, Nashville, Tennessee 37232-0615

We have used a combination of fluorescence anisotropy spectroscopy and fluorescence-based native gel electrophoresis methods to examine the effects of the transcription factor IID-specific subunit TAF130p (TAF145p) upon the TATA box DNA binding properties of TATA box-binding protein (TBP). Purified full-length recombinant TAF130p decreases TBP-TATA DNA complex formation at equilibrium by competing directly with DNA for binding to TBP. Interestingly, we have found that full-length TAF130p is capable of binding multiple molecules of TBP with nanomolar binding affinity. The biological implications of these findings are discussed.

* This work was supported by National Institutes of Health Grants GM52461 and GM5858.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.

Dagger Present address: Molecular Probes, Inc., Eugene, OR 97402.

§ Present address: Argus Research Corp., New York, NY 10006.

Present address: Dept. of Biochemistry and Molecular Genetics, University of Colorado, Health Sciences Center, Denver, CO 80220.

|| To whom correspondence should be addressed. Tel.: 615-322-7007; Fax: 615-322-7236; E-mail: tony.weil@mcmail.vanderbilt.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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