A histone octamer-like structure within TFIID

Nature. 1996 Mar 28;380(6572):356-9. doi: 10.1038/380356a0.


The general transcription factor TFIID nucleates initiation complex formation through direct core promoter binding, commits promoters within chromatin to transcription, and mediates the action of transcriptional activators, a phenomenon that may correlate with enhanced TFIID recruitment or conformational changes in TFIID-promoter complexes. Molecular studies of the multiprotein TFIID complex have identified a primary TATA binding subunit (TBP), TBP-associated factors (TAFs) that interact with and mediate the function of activators and intersubunit interactions but have yielded relatively little insight into the structural organization of the complex or the actual mechanism of transcriptional activation. Here we present biochemical evidence for the structural relevance of histone homologies in the human TFIID subunits hTAF80, hTAF31 and hTAF20/15. Together with analyses of native TFIID complexes and accompanying crystallographic studies, the results suggest that there is a histone octamer-like TAF complex within TFIID.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • DNA-Binding Proteins / chemistry
  • HeLa Cells
  • Histones / chemistry*
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Recombinant Fusion Proteins / chemistry
  • Sequence Alignment
  • TATA-Binding Protein Associated Factors*
  • TATA-Box Binding Protein
  • Trans-Activators / chemistry
  • Transcription Factor TFIID
  • Transcription Factors / chemistry*


  • DNA-Binding Proteins
  • Histones
  • Recombinant Fusion Proteins
  • TAF6 protein, human
  • TAF9 protein, human
  • TATA-Binding Protein Associated Factors
  • TATA-Box Binding Protein
  • Trans-Activators
  • Transcription Factor TFIID
  • Transcription Factors

Associated data

  • GENBANK/U57693