Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family.
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Yang WM, Yao YL, Sun JM, Davie JR, Seto E
Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family.
J Biol Chem. 1997 Oct 31;272(44):28001-7.
- PubMed ID
- 9346952 [ View in PubMed]
- Abstract
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.