ATP-Dependent histone octamer mobilization and histone deacetylation mediated by the Mi-2 chromatin remodeling complex

Biochemistry. 2000 May 9;39(18):5238-45. doi: 10.1021/bi000421t.


The Mi-2 complex has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. Here, we use a purified Mi-2 complex containing six components, Mi-2, Mta 1-like, p66, RbAp48, RPD3, and MBD3, to investigate the capacity of this complex to destabilize histone-DNA interactions and deacetylate core histones. The Mi-2 complex has ATPase activity that is stimulated by nucleosomes but not by free histones or DNA. This nucleosomal ATPase is relatively inefficient, yet is essential to facilitate both translational movement of histone octamers relative to DNA and the efficient deacetylation of the core histones within a mononucleosome. Surprisingly, ATPase activity had no effect on deacetylation of nucleosomal arrays.

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / pharmacology*
  • Animals
  • Autoantigens / metabolism*
  • Centrifugation, Density Gradient
  • Chickens
  • Chromatin / metabolism
  • DNA / analysis
  • DNA Helicases*
  • Electrophoresis, Polyacrylamide Gel
  • Erythrocytes / metabolism
  • Histone Acetyltransferases
  • Histone Deacetylases / metabolism
  • Histones / metabolism*
  • Mi-2 Nucleosome Remodeling and Deacetylase Complex
  • Nucleosomes / enzymology
  • Nucleosomes / metabolism
  • Oocytes / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Xenopus


  • Autoantigens
  • CHD4 protein, human
  • Chromatin
  • Histones
  • Nucleosomes
  • Saccharomyces cerevisiae Proteins
  • Adenosine Triphosphate
  • DNA
  • Acetyltransferases
  • Histone Acetyltransferases
  • Histone Deacetylases
  • Mi-2 Nucleosome Remodeling and Deacetylase Complex
  • Adenosine Triphosphatases
  • DNA Helicases