A positive role for histone acetylation in transcription factor access to nucleosomal DNA

Cell. 1993 Jan 15;72(1):73-84. doi: 10.1016/0092-8674(93)90051-q.

Abstract

Acetylation of the N-terminal tails of the core histones directly facilitates the recognition by TFIIIA of the 5S RNA gene within model chromatin templates. This effect is independent of a reduction in the extent of histone-DNA interactions or a change in DNA helical repeat; it is also independent of whether a histone tetramer or octamer inhibits TFIIIA binding. Removal of the N-terminal tails from the core histones also facilitates the association of TFIIIA with nucleosomal templates. We suggest that the histone tails have a major role in restricting transcription factor access to DNA and that their acetylation releases this restriction by directing dissociation of the tails from DNA and/or inducing a change in DNA configuration on the histone core to allow transcription factor binding. Acetylation of core histones might be expected to exert a major influence on the accessibility of chromatin to regulatory molecules.

MeSH terms

  • Acetylation
  • Animals
  • Chickens
  • DNA, Ribosomal / metabolism*
  • HeLa Cells
  • Histones / metabolism*
  • Humans
  • Nucleosomes / metabolism*
  • RNA, Ribosomal, 5S / genetics*
  • Transcription Factor TFIIA
  • Transcription Factors / metabolism*
  • Xenopus
  • Xenopus laevis

Substances

  • DNA, Ribosomal
  • Histones
  • Nucleosomes
  • RNA, Ribosomal, 5S
  • Transcription Factor TFIIA
  • Transcription Factors