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J. Biol. Chem., Vol. 279, Issue 31, 32401-32406, July 30, 2004
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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
¶ 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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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. ![]()
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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]
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