Inhibition of TATA binding protein dimerization by RNA polymerase III transcription initiation factor Brf1

Diane E. Alexander, David J. Kaczorowski, Amy J. Jackson-Fisher, Drew M. Lowery, Sara J. Zanton, B. Franklin Pugh

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)32401-32406
Number of pages6
JournalJournal of Biological Chemistry
Volume279
Issue number31
DOIs
StatePublished - Jul 30 2004

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Alexander, D. E., Kaczorowski, D. J., Jackson-Fisher, A. J., Lowery, D. M., Zanton, S. J., & Pugh, B. F. (2004). Inhibition of TATA binding protein dimerization by RNA polymerase III transcription initiation factor Brf1. Journal of Biological Chemistry, 279(31), 32401-32406. https://doi.org/10.1074/jbc.M405782200