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Originally published In Press as doi:10.1074/jbc.M908988199 on March 9, 2000
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J Biol Chem, Vol. 275, Issue 20, 15254-15264, May 19, 2000

Cloning and Characterization of a Novel Human Class I Histone Deacetylase That Functions as a Transcription Repressor*

Erding HuDagger §, Zunxuan ChenDagger , Todd FredricksonDagger , Yuan Zhu, Robert Kirkpatrick||, Gui-Feng Zhang||, Kyung Johanson||, Chiu-Mei Sung**, Ronggang LiuDagger Dagger , and James Winkler**

From the Departments of Dagger  Renal Pharmacology, ** Oncology,  Molecular Biology, Dagger Dagger  Medicinal Chemistry, and || Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19403

Histone acetylation alters chromatin state by modifying lysines on histone and plays an important role in modulating gene transcription. A dynamic balance of histone acetylation/deacetylation is maintained by histone acetyltransferases and histone deacetylases. Emerging evidence suggests that a family of histone deacetylases may exist to regulate diverse cellular functions, including chromatin structure, gene expression, cell cycle progression, and oncogenesis. We describe here a novel human histone deacetylase, named HDAC8, cloned from human kidney. HDAC8 encodes 377 amino acid residues and shares extensive homology to several known HDACs, in particular a histone deacetylase from Arabidopsis thaliana. Northern blot analyses revealed that HDAC8 expression pattern for HDAC8 is distinct from that for HDAC1 and HDAC3, and expression of HDAC8 mRNA occurs in multiple organs including heart, lung, kidney, and pancreas. HDAC8 mRNA was also observed in several cell lines derived from cancerous tissues. When expressed in HEK293 cells, HDAC8 exhibited deacetylase activity toward acetylated histone, indicating that this protein is a bona fide histone deacetylase. Its histone deacetylase activity was inhibited by trichostatin and other known histone deacetylase inhibitors. Furthermore, active recombinant HDAC8 was expressed and purified from Escherichia coli. When ectopically expressed in cells, HDAC8 was found to be localized to the nucleus. Co-transfection experiments demonstrated that expression of HDAC8 repressed a viral SV40 early promoter activity. These results indicate that HDAC8 is a novel member of the histone deacetylase family, which may play a role in the development of a broad range of tissues and potentially in the etiology of cancer.

* 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/EMBL Data Bank with accession number(s) AF230097.

§ To whom correspondence should be addressed: Dept. of Renal Pharmacology, SmithKline Beecham Pharmaceuticals, 709 Swedeland Rd., King of Prussia, PA 19403. Tel.: 610-270-6087; Fax: 610-270-5681; E-mail: erding_hu-1@sbphrd.com.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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