Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC

Science. 1999 Dec 10;286(5447):2151-3. doi: 10.1126/science.286.5447.2151.

Abstract

TBP (TATA-binding protein)-associated factors (TAF(II)s) are components of large multiprotein complexes such as TFIID, TFTC, STAGA, PCAF/GCN5, and SAGA, which play a key role in the regulation of gene expression by RNA polymerase II. The structures of TFIID and TFTC have been determined at 3.5-nanometer resolution by electron microscopy and digital image analysis of single particles. Human TFIID resembles a macromolecular clamp that contains four globular domains organized around a solvent-accessible groove of a size suitable to bind DNA. TFTC is larger and contains five domains, four of which are similar to TFIID.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Binding Proteins / analysis
  • DNA-Binding Proteins / chemistry*
  • HeLa Cells
  • Humans
  • Image Processing, Computer-Assisted
  • Microscopy, Electron
  • Models, Molecular*
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary
  • TATA-Binding Protein Associated Factors*
  • Transcription Factor TFIID
  • Transcription Factors / analysis
  • Transcription Factors / chemistry*
  • Transcription Factors, TFII / chemistry*

Substances

  • DNA-Binding Proteins
  • TAF10 protein, human
  • TATA-Binding Protein Associated Factors
  • Transcription Factor TFIID
  • Transcription Factors
  • Transcription Factors, TFII