Structural similarity between TAFs and the heterotetrameric core of the histone octamer

Nature. 1996 Mar 28;380(6572):316-22. doi: 10.1038/380316a0.


A complex of two TFIID TATA box-binding protein-associated factors (TA FIIs) is described at 2.0A resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short alpha-helices flanking a long central alpha-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chickens
  • Crystallography, X-Ray
  • DNA-Binding Proteins / chemistry
  • Drosophila
  • Drosophila Proteins*
  • Escherichia coli
  • Histones / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • RNA Polymerase II / metabolism
  • Recombinant Proteins / chemistry
  • Sequence Alignment
  • TATA-Binding Protein Associated Factors*
  • TATA-Box Binding Protein
  • Trans-Activators / chemistry*
  • Transcription Factor TFIID
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism


  • DNA-Binding Proteins
  • Drosophila Proteins
  • Histones
  • Recombinant Proteins
  • TATA-Binding Protein Associated Factors
  • TATA-Box Binding Protein
  • Taf6 protein, Drosophila
  • Trans-Activators
  • Transcription Factor TFIID
  • Transcription Factors
  • e(y)1 protein, Drosophila
  • RNA Polymerase II