Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein

Cell. 1995 Sep 8;82(5):857-67. doi: 10.1016/0092-8674(95)90483-2.

Abstract

TFIIB is an essential component of the machinery that transcribes protein-coding genes. The three-dimensional structure of the human TFIIB core domain (TFIIBc) has been determined using multidimensional heteronuclear magnetic resonance spectroscopy. The molecule consists of two direct repeats that adopt similar alpha-helical folds, conferring pseudo-twofold symmetry. An extensive, central basic surface including an amphipathic alpha helix is critical to the function of TFIIB as a bridge between the TBP-promoter complex and RNA polymerase II and associated general and regulatory transcription factors. Similarities between the TFIIBc and cyclin A folds indicate that elements of the eukaryotic cell cycle control apparatus evolved from more fundamental transcriptional control components, demonstrating a link between the transcription and cell cycle molecular machineries.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites / genetics
  • Cyclins / genetics*
  • DNA / metabolism
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Image Processing, Computer-Assisted
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Promoter Regions, Genetic / genetics
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • TATA Box / genetics*
  • TATA-Box Binding Protein
  • Transcription Factor TFIIB
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism*
  • Transcription Factors / ultrastructure
  • Transcription, Genetic / genetics

Substances

  • Cyclins
  • DNA-Binding Proteins
  • TATA-Box Binding Protein
  • Transcription Factor TFIIB
  • Transcription Factors
  • DNA