The histone fold is a key structural motif of transcription factor TFIID

Trends Biochem Sci. 2001 Apr;26(4):250-7. doi: 10.1016/s0968-0004(00)01741-2.

Abstract

Transcription factor TFIID is a multiprotein complex composed of the TATA binding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase II. The subunit composition of this factor is highly conserved from yeast to mammals. X-ray crystallography and biochemical experiments have shown that the histone fold motif mediates many of the subunit interactions within this complex. These results, together with electron microscopy and yeast genetics, provide insights into the overall organization of this complex.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Histones / chemistry
  • Histones / metabolism*
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Sequence Homology, Amino Acid
  • Transcription Factor TFIID
  • Transcription Factors, TFII / chemistry
  • Transcription Factors, TFII / metabolism*

Substances

  • Histones
  • Transcription Factor TFIID
  • Transcription Factors, TFII