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The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities.

Cell | Oct 16, 1998

http://www.ncbi.nlm.nih.gov/pubmed/9790534

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.

Pubmed ID: 9790534 RIS Download

Mesh terms: Adenosine Triphosphatases | Adenosine Triphosphate | Autoantigens | Chromatin | DNA Helicases | Dermatomyositis | HeLa Cells | Histone Deacetylases | Histones | Humans | Mi-2 Nucleosome Remodeling and Deacetylase Complex | Multienzyme Complexes | Nucleosomes | Protein Binding | Zinc Fingers

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Associated grants

  • Agency: NIGMS NIH HHS, Id: 1F32GM19515-01
  • Agency: NIGMS NIH HHS, Id: GM-48518

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