The TATA-binding protein (TBP) is a general transcription factor that binds to a DNA sequence called the TATA box. This DNA sequence is found about 30 base pairs upstream of the transcription start site in some eukaryotic gene promoters .

Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA …

Dec 21, 2018 · We used cryo-electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box-binding protein (TBP) loading onto promoter DNA.

The TATA-binding protein (TBP) is an essential component of the transcription initiation complex TFIID and is required for gene expression. We identify two discrete regions mediating MYC-TBP interactions using structural, biochemical and cellular approaches.

Jul 7, 2021 · TBP binds and bends DNA, and directs adjacent binding of the transcription factors TFIIA and TFIIB for PIC assembly. Here, we show that yeast TBP can bind to a nucleosome containing the Widom-601 sequence and that TBP–nucleosome binding is stabilized by TFIIA.

We present a comprehensive study of the evolutionary history of TBP and its interaction partners across all domains of life, including viruses. Our analysis reveals the molecular determinants and suggests a unified and multi-stage evolutionary model for the functional innovations of TBP.

TBP in yeast are summarized in Table 1. Here we review our current understanding of the eu-karyotic TBP-associated proteins and their roles in regu-lation of gene expression. We describe evidence that rela-tively small pools of each of the TBP-associated proteins interact with and regulate a large cellular pool of TBP in

Apr 1, 2020 · This paper also defines the structural transitions of Lobe A during TBP loading onto the promoter and proposes a model of inhibition release for the different functional surfaces of TBP that relies on downstream promoter binding by Lobe C and TFIIA interactions with Lobe B.

Here we present the crystal structure (1.97 Å) and NMR analysis of yeast TAF1 N-terminal domains TAND1 and TAND2 when bound to yeast TBP, together with mutational data.

Human TFIID is a trilobed (lobes A, B, and C) complex composed of TATA box binding–protein (TBP) and 13 evolutionarily conserved TBP-associated factors (TAF1 to TAF13), with six TAFs present in two copies.