Isolation and characterization of mammalian HDAC10, a novel histone deacetylase.
Acetylation of histone core particles plays an important role in modulating chromatin structure and gene expression. The acetylation status of the histone tails is determined by two opposing enzymatic activities, histone acetyltransferases and histone deacetylases (HDACs). Here we describe the isolation and characterization of HDAC10, a novel class II histone deacetylase. Molecular cloning and Northern blot analyses reveal that the HDAC10 transcript is widely expressed and subjected to alternative splicing. HDAC10 is both nuclear and cytoplasmic, a feature reminiscent of HDACs 4, 5, and 7. Distinct from other family members, HDAC10 harbors an amino-terminal catalytic domain and a carboxyl pseudo-repeat that shares significant homology with its catalytic domain. Mutational analysis reveals that transcriptional repression by HDAC10 requires its intrinsic histone deacetylase activity. Taken together, HDAC10 represents a distinct HDAC that may play a role in transcription regulation.
Kao
Hung-Ying
HY
Department of Biochemistry, School of Medicine, Case Western Reserve University, the Research Institute of University Hospitals of Cleveland, and the Comprehensive Cancer Center of CWRU and UHC, Cleveland, Ohio 44106, USA. hxk43@po.cwru.edu
Lee
Chih-Hao
CH
Komarov
Andrei
A
Han
Chris C
CC
Evans
Ronald M
RM
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002467:Cell Nucleus / Q000201:enzymology; D003593:Cytoplasm / Q000201:enzymology; D018076:DNA, Complementary / Q000302:isolation & purification; D006655:Histone Deacetylases / Q000235:genetics / Q000302:isolation & purification* / Q000502:physiology; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D014158:Transcription, Genetic
D018076:DNA, Complementary; D006655:Histone Deacetylases