Molecular structure of promoter-bound yeast TFIID

Nat Commun. 2018 Nov 7;9(1):4666. doi: 10.1038/s41467-018-07096-y.


Transcription preinitiation complex assembly on the promoters of protein encoding genes is nucleated in vivo by TFIID composed of the TATA-box Binding Protein (TBP) and 13 TBP-associate factors (Tafs) providing regulatory and chromatin binding functions. Here we present the cryo-electron microscopy structure of promoter-bound yeast TFIID at a resolution better than 5 Å, except for a flexible domain. We position the crystal structures of several subunits and, in combination with cross-linking studies, describe the quaternary organization of TFIID. The compact tri lobed architecture is stabilized by a topologically closed Taf5-Taf6 tetramer. We confirm the unique subunit stoichiometry prevailing in TFIID and uncover a hexameric arrangement of Tafs containing a histone fold domain in the Twin lobe.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA, Fungal / chemistry
  • DNA, Fungal / metabolism
  • Models, Molecular
  • Promoter Regions, Genetic / genetics*
  • Protein Binding
  • Protein Subunits / chemistry
  • Protein Subunits / isolation & purification
  • Protein Subunits / metabolism
  • Saccharomyces cerevisiae / metabolism
  • Transcription Factor TFIID / chemistry*
  • Transcription Factor TFIID / isolation & purification
  • Transcription Factor TFIID / metabolism*
  • Yeasts / metabolism*


  • DNA, Fungal
  • Protein Subunits
  • Transcription Factor TFIID