Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 279, Issue 31, Pages 32401-32406Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M405782200
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Funding
- NIGMS NIH HHS [R01 GM059055, GM059055] Funding Source: Medline
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The Brf1 subunit of TFIIIB plays an important role in recruiting the TATA-binding protein (TBP) to the upstream 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.
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