Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities

Mol Cell. 2003 Dec;12(6):1599-606. doi: 10.1016/s1097-2765(03)00499-4.

Abstract

ATP-dependent chromatin remodeling activities function to manipulate chromatin structure during gene regulation. One of the ways in which they do this is by altering the positions of nucleosomes along DNA. Here we provide support for the ability of these complexes to move nucleosomes into positions in which DNA is unraveled from one edge. This is expected to result in the loss of histone-DNA contacts that are important for retention of one H2A/H2B dimer within the nucleosome. Consistent with this we find that several chromatin remodeling complexes are capable of catalyzing the exchange of H2A/H2B dimers between chromatin fragments in an ATP-dependent reaction. This provides eukaryotes with additional means by which they may manipulate chromatin structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Chromatin / metabolism*
  • Chromosomal Proteins, Non-Histone / metabolism
  • DNA, Fungal
  • Dimerization
  • Drosophila melanogaster
  • Fungal Proteins / metabolism
  • Histones / metabolism*
  • Models, Molecular
  • Nucleic Acid Conformation
  • Nucleosomes / metabolism
  • Protein Structure, Tertiary
  • Transcription Factors / metabolism
  • Xenopus laevis

Substances

  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • DNA, Fungal
  • Fungal Proteins
  • Histones
  • Nucleosomes
  • Transcription Factors
  • Adenosine Triphosphate
  • Adenosine Triphosphatases