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, 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.
Mesh Terms:
Amino Acid Sequence, Cloning, Molecular, DNA, Complementary, Hela Cells, Histone Deacetylases, Humans, Molecular Sequence Data, Multigene Family, Peptide YY, Protein Binding, Sequence Homology, Amino Acid
Amino Acid Sequence, Cloning, Molecular, DNA, Complementary, Hela Cells, Histone Deacetylases, Humans, Molecular Sequence Data, Multigene Family, Peptide YY, Protein Binding, Sequence Homology, Amino Acid
J. Biol. Chem.
Date: Oct. 31, 1997
PubMed ID: 9346952
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