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.
Yang
W M
WM
Moffitt Cancer Center and Research Institute, the Department of Medical Microbiology and Immunology, College of Medicine, University of South Florida, Tampa, Florida 33612, USA.
Yao
Y L
YL
Sun
J M
JM
Davie
J R
JR
Seto
E
E
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006367:HeLa Cells; D006655:Histone Deacetylases / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family; D019894:Peptide YY / Q000378:metabolism; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D000099186:Histone Deacetylase 3
D018076:DNA, Complementary; D006655:Histone Deacetylases; D019894:Peptide YY; D000099186:Histone Deacetylase 3