A Multiple Subunit Mi-2 Histone Deacetylase From Xenopus Laevis Cofractionates With an Associated Snf2 Superfamily ATPase

Curr Biol. 1998 Jul 2;8(14):843-6. doi: 10.1016/s0960-9822(98)70328-8.

Abstract

Chromatin structure plays a crucial regulatory role in the control of gene expression. In eukaryotic nuclei, enzymatic complexes can alter this structure by both targeted covalent modification and ATP-dependent chromatin remodeling. Modification of histone amino termini by acetyltransferases and deacetylases correlates with transcriptional activation and repression [1-3], cell growth [4], and tumorigenesis [5]. Chromatin-remodeling enzymes of the Snf2 superfamily use ATP hydrolysis to restructure nucleosomes and chromatin, events which correlate with activation of transcription [6,7]. We purified a multi-subunit complex from Xenopus laevis eggs which contains six putative subunits including the known deacetylase subunits Rpd3 and RbAp48/p46 [8] as well as substoichiometric quantities of the deacetylase-associated protein Sin3 [9-13]. In addition, we identified one of the other components of the complex to be Mi-2, a Snf2 superfamily member previously identified as an autoantigen in the human connective tissue disease dermatomyositis [14,15]. We found that nucleosome-stimulated ATPase activity precisely copurified with both histone deacetylase activity and the deacetylase enzyme complex. This association of a histone deacetylase with a Snf2 superfamily ATPase suggests a functional link between these two disparate classes of chromatin regulators.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / isolation & purification
  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Autoantigens / chemistry*
  • Autoantigens / immunology
  • Autoantigens / isolation & purification
  • DNA Helicases*
  • Dermatomyositis / enzymology
  • Dermatomyositis / immunology
  • Female
  • Histone Deacetylases / chemistry*
  • Histone Deacetylases / isolation & purification
  • Histone Deacetylases / metabolism*
  • Humans
  • Macromolecular Substances
  • Mi-2 Nucleosome Remodeling and Deacetylase Complex
  • Oocytes / chemistry
  • Oocytes / enzymology*
  • Xenopus laevis

Substances

  • Autoantigens
  • CHD4 protein, human
  • Macromolecular Substances
  • Histone Deacetylases
  • Mi-2 Nucleosome Remodeling and Deacetylase Complex
  • Adenosine Triphosphatases
  • DNA Helicases

Associated data

  • GENBANK/AF059185