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Updated: Oct 18, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
The structural basis for the oriented assembly of a TBP/TFB/promoter complex
O Littlefield1, Y Korkhin, P B Sigler
1Department of Molecular Biophysics, Yale University, New Haven CT 06511, USA.
Abstract:
Recently the definition of the metazoan RNA polymerase II and archaeal core promoters has been expanded to include a region immediately upstream of the TATA box called the B recognition element (BRE), so named because eukaryal transcription factor TFIIB and its archaeal orthologue TFB interact with the element in a sequence-specific manner. Here we present the 2.4-A crystal structure of archaeal TBP and the C-terminal core of TFB (TFB(c)) in a complex with an extended TATA-box-containing promoter that provides a detailed picture of the stereospecific interactions between the BRE and a helix-turn-helix motif in the C-terminal cyclin repeat of TFB(c). This interaction is important in determining the level of basal transcription and explicitly defines the direction of transcription.
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