Three-dimensional structure of the human TFIID-IIA-IIB complex

Science. 1999 Dec 10;286(5447):2153-6. doi: 10.1126/science.286.5447.2153.

Abstract

The multisubunit transcription factor IID (TFIID) is an essential component of the eukaryotic RNA polymerase II machinery that works in concert with TFIIA (IIA) and TFIIB (IIB) to assemble initiation complexes at core eukaryotic promoters. Here the structures of human TFIID and the TFIID-IIA-IIB complex that were obtained by electron microscopy and image analysis to 35 angstrom resolution are presented. TFIID is a trilobed, horseshoe-shaped structure, with TFIIA and TFIIB bound on opposite lobes and flanking a central cavity. Antibody studies locate the TATA-binding protein (TBP) between TFIIA and TFIIB at the top of the cavity that most likely encompasses the TATA DNA binding region of the supramolecular complex.

Publication types

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

MeSH terms

  • Binding Sites
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • HeLa Cells
  • Humans
  • Image Processing, Computer-Assisted
  • Microscopy, Electron
  • Promoter Regions, Genetic
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • TATA-Box Binding Protein
  • Transcription Factor TFIIA
  • Transcription Factor TFIIB
  • Transcription Factor TFIID
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism
  • Transcription Factors, TFII / chemistry*
  • Transcription Factors, TFII / metabolism
  • Transcription, Genetic

Substances

  • DNA-Binding Proteins
  • Recombinant Proteins
  • TATA-Box Binding Protein
  • Transcription Factor TFIIA
  • Transcription Factor TFIIB
  • Transcription Factor TFIID
  • Transcription Factors
  • Transcription Factors, TFII
  • DNA