Promoter Recognition: Putting TFIID on the Spot

Trends Cell Biol. 2019 Sep;29(9):752-763. doi: 10.1016/j.tcb.2019.06.004. Epub 2019 Jul 9.

Abstract

Basal transcription factor TFIID connects transcription activation to the assembly of the RNA polymerase II preinitiation complex at the core promoter of genes. The mechanistic understanding of TFIID function and dynamics has been limited by the lack of high-resolution structures of the holo-TFIID complex. Recent cryo-electron microscopy studies of yeast and human TFIID complexes provide insight into the molecular organization and structural dynamics of this highly conserved transcription factor. Here, we discuss how these TFIID structures provide new paradigms for: (i) the dynamic recruitment of TFIID; (ii) the binding of TATA-binding protein (TBP) to promoter DNA; (iii) the multivalency of TFIID interactions with (co)activators, nucleosomes, or promoter DNA; and (iv) the opportunities for regulation of TBP turnover and promoter dynamics.

Keywords: RNA polymerase; TFIID; basal transcription factors; core promoters; cryo-EM; transcription regulation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cryoelectron Microscopy
  • DNA / chemistry*
  • DNA / ultrastructure
  • Humans
  • Models, Molecular
  • Promoter Regions, Genetic*
  • Protein Conformation*
  • Schizosaccharomyces / chemistry
  • TATA-Box Binding Protein / metabolism
  • Transcription Factor TFIID / chemistry*
  • Transcription Factor TFIID / ultrastructure
  • Transcriptional Activation

Substances

  • TATA-Box Binding Protein
  • Transcription Factor TFIID
  • DNA