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Originally published In Press as doi:10.1074/jbc.M405782200 on June 9, 2004

J. Biol. Chem., Vol. 279, Issue 31, 32401-32406, July 30, 2004
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Inhibition of TATA Binding Protein Dimerization by RNA Polymerase III Transcription Initiation Factor Brf1*

Diane E. Alexander{ddagger}, David J. Kaczorowski§, Amy J. Jackson-Fisher, Drew M. Lowery||, Sara J. Zanton, and B. Franklin Pugh**

From the Center for Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802

The Brf1 subunit of TFIIIB plays an important role in recruiting the TATA-binding protein (TBP) to the up-stream region of genes transcribed by RNA polymerase III. When TBP is not bound to promoters, it sequesters its DNA binding domain through dimerization. Promoter assembly factors therefore might be required to dissociate TBP into productively binding monomers. Here we show that Saccharomyces cerevisiae Brf1 induces TBP dimers to dissociate. The high affinity TBP binding domain of Brf1 is not sufficient to promote TBP dimer dissociation but in addition requires the TFIIB homology domain of Brf1. A model is proposed to explain how two distinct functional domains of Brf1 work in concert to dissociate TBP into monomers.


Received for publication, May 24, 2004

* This work was supported by National Institutes of Health Grant GM059055. 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.

{ddagger} Current address: Dept. of Medicine, Washington University School of Medicine, St. Louis, MO 63110.

§ Current address: Dept. of Surgery, PRESB F1263, University of Pittsburgh, Pittsburgh, PA 15260.

Current address: Dept. of Pathology, Yale School of Medicine, 310 Cedar St., BML-342, New Haven, CT 06510.

|| Current address: Center for Cancer Research, Dept. of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.

** To whom correspondence should be addressed: 452 N. Frear Laboratory, Dept. of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16803. Fax: 814-863-8595; E-mail: bfp2{at}psu.edu.


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M. Bendjennat and P. A. Weil
The Transcriptional Repressor Activator Protein Rap1p Is a Direct Regulator of TATA-binding Protein
J. Biol. Chem., March 28, 2008; 283(13): 8699 - 8710.
[Abstract] [Full Text] [PDF]




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