Characterization of a human <i>RPD3</i> ortholog, HDAC3

DOI Web Site 被引用文献3件
  • Stephane Emiliani
    Picower Institute for Medical Research, Manhasset, NY 11030; and Gladstone Institute for Virology and Immunology, University of California, San Francisco, CA 94103
  • Wolfgang Fischle
    Picower Institute for Medical Research, Manhasset, NY 11030; and Gladstone Institute for Virology and Immunology, University of California, San Francisco, CA 94103
  • Carine Van Lint
    Picower Institute for Medical Research, Manhasset, NY 11030; and Gladstone Institute for Virology and Immunology, University of California, San Francisco, CA 94103
  • Yousef Al-Abed
    Picower Institute for Medical Research, Manhasset, NY 11030; and Gladstone Institute for Virology and Immunology, University of California, San Francisco, CA 94103
  • Eric Verdin
    Picower Institute for Medical Research, Manhasset, NY 11030; and Gladstone Institute for Virology and Immunology, University of California, San Francisco, CA 94103

抄録

<jats:p> Histone acetylation levels in cells result from a dynamic equilibrium between competing histone acetylases and deacetylases. Changes in histone acetylation levels occur during both transcriptional activation and silencing. Cloning of the cDNA for a human histone deacetylase (HDAC1) has shown that it represents a human ortholog of the yeast transcriptional regulator <jats:italic>RPD3</jats:italic> . We have screened the expressed sequence tag database (National Center for Biotechnology Information) with the yeast RPD3 sequence and identified a human ortholog of <jats:italic>RPD3</jats:italic> , HDAC3. This cDNA encodes a protein of 428 amino acids with 58% sequence identity with HDAC1p. By using a specific polyclonal antiserum recognizing the C-terminal domain of HDAC3p and Western blotting, we detected a single ∼49-kDa band in several tumor cell lines. HDAC3p is expressed predominantly in the nuclear compartment. Immunoprecipitation experiments with either an antiserum against HDAC3p or an anti-FLAG antiserum and a flagged HDAC3 cDNA showed that HDAc3p exhibits deacetylase activity both on free histones and on purified nucleosomes. This deacetylase activity is inhibited by trichostatin, trapoxin, and butyrate <jats:italic>in vitro</jats:italic> to the same degree as the deacetylase activity associated to HDAC1p. These observations identify another member of a growing family of human HDAC genes. </jats:p>

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