ISOLATION AND CHARACTERIZATION OF CDNAS CORRESPONDING TO AN ADDITIONAL MEMBER OF THE HUMAN HISTONE DEACETYLASE GENE FAMILY

Several human cDNAs encoding a histone deacetylase protein, HDAC3, hav e been isolated. Analysis of the predicted amino acid sequence of HDAC 3 revealed an open reading frame of 428 amino acids with a predicted m olecular mass of 49 kDa. The HDAC3 protein is 50% identical in DNA seq uence and 53% identical in protein sequence compared with the previous ly cloned human HDAC1, Comparison of the HDAC3 sequence with human HDA C2 also yielded similar results, with 51% identity in DNA sequence and 52% identity in protein sequence. The expressed HDAC3 protein is func tionally active because it possesses histone deacetylase activity, rep resses transcription when tethered to a promoter, and binds transcript ion factor YY1. Similar to HDAC1 and HDAC2, HDAC3 is ubiquitously expr essed in many different cell types.