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Originally published In Press as doi:10.1074/jbc.M108931200 on October 24, 2001

J. Biol. Chem., Vol. 277, Issue 1, 187-193, January 4, 2002
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Isolation and Characterization of Mammalian HDAC10, a Novel Histone Deacetylase*

Hung-Ying KaoDagger §, Chih-Hao Lee, Andrei KomarovDagger , Chris C. HanDagger , and Ronald M. Evans||

From the Dagger  Department of Biochemistry, School of Medicine, Case Western Reserve University (CWRU), the Research Institute of University Hospitals of Cleveland (UHC), and the Comprehensive Cancer Center of CWRU and UHC, Cleveland, Ohio 44106 and the  Howard Hughes Medical Institute, Gene Expression Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037

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.

* This work was supported by a start-up fund (to H. Y. K.) and National Institutes of Health Grant HD27183 (to R. M. E.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF407272 (HDAC10alpha ) and AF407273 (HDAC10beta ).

§ Recipient of the James T. Pardee-Carl A. Gerstacker Assistant Professor of Cancer Research Faculty, and Chair in Cancer Research at CWRU Cancer Center. To whom correspondence may be addressed: Dept. of Biochemistry, Case Western Reserve University, 10900 Euclid Ave., Cleveland, OH 44106. Tel.: 216-844-7572; Fax: 216-368-3419; E-mail: hxk43@po.cwru.edu.

|| Investigator of the Howard Hughes Medical Institute at the Salk Institute for Biological Studies, and March of Dimes Chair in Molecular and Developmental Biology. To whom correspondence may be addressed: The Howard Hughes Medical Institute, Gene Expression Laboratory, The Salk Institute for Biological Studies, 10010 Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-453-4100, Ext. 1585; Fax: 858-455-1349; E-mail: evans@salk.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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