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    J Biol Chem. 1997 Oct 31;272(44):28001-7.

    Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family.

    Yang WM, Yao YL, Sun JM, Davie JR, Seto E.

    Moffitt Cancer Center and Research Institute, the Department of Medical Microbiology and Immunology, College of Medicine, University of South Florida, Tampa, Florida 33612, USA.

    Several human cDNAs encoding a histone deacetylase protein, HDAC3, have been isolated. Analysis of the predicted amino acid sequence of HDAC3 revealed an open reading frame of 428 amino acids with a predicted molecular mass of 49 kDa. The HDAC3 protein is 50% identical in DNA sequence and 53% identical in protein sequence compared with the previously cloned human HDAC1. Comparison of the HDAC3 sequence with human HDAC2 also yielded similar results, with 51% identity in DNA sequence and 52% identity in protein sequence. The expressed HDAC3 protein is functionally active because it possesses histone deacetylase activity, represses transcription when tethered to a promoter, and binds transcription factor YY1. Similar to HDAC1 and HDAC2, HDAC3 is ubiquitously expressed in many different cell types.

    PMID: 9346952 [PubMed - indexed for MEDLINE]

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