The Dermatomyositis-Specific Autoantigen Mi2 Is a Component of a Complex Containing Histone Deacetylase and Nucleosome Remodeling Activities

Cell. 1998 Oct 16;95(2):279-89. doi: 10.1016/s0092-8674(00)81758-4.

Abstract

Histone acetylation and deacetylation were found to be catalyzed by structurally distinct, multisubunit complexes that mediate, respectively, activation and repression of transcription. ATP-dependent nucleosome remodeling, mediated by different multisubunit complexes, was thought to be involved only in transcription activation. Here we report the isolation of a protein complex that contains both histone deacetylation and ATP-dependent nucleosome remodeling activities. The complex contains the histone deacetylases HDAC1/2, histone-binding proteins, the dermatomyositis-specific autoantigen Mi2beta, a polypeptide related to the metastasis-associated protein 1, and a novel polypeptide of 32 kDa. Patients with dermatomyositis have a high rate of malignancy. The finding that Mi2beta exists in a complex containing histone deacetylase and nucleosome remodeling activities suggests a role for chromatin reorganization in cancer metastasis.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases*
  • Adenosine Triphosphate / metabolism
  • Autoantigens / metabolism*
  • Chromatin / metabolism
  • DNA Helicases*
  • Dermatomyositis / immunology*
  • Dermatomyositis / metabolism*
  • HeLa Cells
  • Histone Deacetylases / metabolism*
  • Histones / metabolism
  • Humans
  • Mi-2 Nucleosome Remodeling and Deacetylase Complex
  • Multienzyme Complexes / metabolism
  • Nucleosomes / enzymology*
  • Protein Binding / physiology
  • Zinc Fingers / physiology

Substances

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