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J. Biol. Chem., Vol. 279, Issue 25, 26257-26265, June 18, 2004

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The Basic Leucine Zipper Domain of c-Jun Functions in Transcriptional Activation through Interaction with the N Terminus of Human TATA-binding Protein-associated Factor-1 (Human TAF_II250)^*

Tricia N. Lively, Tuan N. Nguyen, Shelly K. Galasinski¶, and James A. Goodrich, Recipient of a scholarship from the Pew Charitable Trusts||

From the Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309-0215

We previously reported that c-Jun binds directly to the N-terminal 163 amino acids of Homo sapiens TATA-binding protein-associated factor-1 (hsTAF1), causing a derepression of transcription factor IID (TFIID)-driven transcription (Lively, T. N., Ferguson, H. A., Galasinski, S. K., Seto, A. G., and Goodrich, J. A. (2001) J. Biol. Chem. 276, 25582–25588). This region of hsTAF1 binds TATA-binding protein to repress TFIID DNA binding and transcription. Here we show that the basic leucine zipper domain of c-Jun, which allows for DNA binding and homodimerization, is necessary and sufficient for interaction with hsTAF1. Interestingly, the isolated basic leucine zipper domain of c-Jun was able to derepress TFIID-directed basal transcription in vitro. Moreover, when the N-terminal region of hsTAF1 was added to in vitro transcription reactions and overexpressed in cells, it blocked c-Jun activation. c-Fos, another basic leucine zipper protein, did not interact with hsTAF1, but c-Fos/c-Jun heterodimers did bind the N terminus of hsTAF1. Our studies show that, in addition to dimerization and DNA binding, the well characterized basic leucine zipper domain of c-Jun functions in transcriptional activation by binding to the N terminus of hsTAF1 to derepress transcription.

Received for publication, January 27, 2004 , and in revised form, April 14, 2004.

^* This work was supported in part by United States Public Health Service Grant GM-55235 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported in part by National Institutes of Health Predoctoral Training Grant T32 GM07135. Present address: Div. of Cell Biology, Dept. of Pediatrics, National Jewish Medical and Research Center, Denver, CO 80206.

Supported in part by National Institutes of Health Predoctoral Training Grant T32 GM08759.

^¶ Present address: Genetic Counseling Program, University of North Carolina, 119 McIver, Greensboro, NC 27402.

^|| To whom correspondence should be addressed: Dept. of Chemistry and Biochemistry, University of Colorado, 215 UCB, Boulder, CO 80309-0215. Tel.: 303-492-3273; Fax: 303-492-5894; E-mail: james.goodrich{at}colorado.edu.

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