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Reference: Kassavetis GA, et al. (2006) Mapping the principal interaction site of the Brf1 and Bdp1 subunits of Saccharomyces cerevisiae TFIIIB. J Biol Chem 281(20):14321-9

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Abstract

The Brf1 subunit of the central RNA polymerase (pol) III transcription initiation factor TFIIIB is bipartite: its N-terminal TFIIB-related half is principally responsible for recruiting pol III to the promoter and for promoter opening near the transcriptional start site, while its pol III-specific C-terminal half contributes most of the affinities that hold the 3 subunits of TFIIIB together. Here, the principal attachment site of Brf1 for the Bdp1 subunit of TFIIIB has been mapped by a combination of structure-informed, site-directed mutagenesis and photochemical protein-DNA cross-linking. A 66-amino acid segment of Brf1 is shown to serve as a two-sided adhesive surface, with the side chains projecting away from its extended interface with TBP anchoring Bdp1 binding. An extensive collection of N-terminal, C-terminal and internal deletion proteins has been used to demarcate the interacting Bdp1 domain to a 66 amino acid segment that includes this subunit's SANT domain and is phylogenetically the most conserved region of Bdp1.

Reference Type
Journal Article
Authors
Kassavetis GA, Driscoll R, Geiduschek EP
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