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Originally published In Press as doi:10.1074/jbc.M206528200 on October 18, 2002

J. Biol. Chem., Vol. 278, Issue 3, 1841-1847, January 17, 2003
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Histone Deacetylase 3 Binds to and Regulates the Multifunctional Transcription Factor TFII-I*

Yu-Der WenDagger , W. Douglas CressDagger , Ananda L. Roy§, and Edward SetoDagger

From the Dagger  H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, Florida 33612 and the § Department of Pathology, Tufts University School of Medicine, Boston, Massachusetts 02111

Histone deacetylase 3 (HDAC3) is one of four members of the human class I histone deacetylases that are implicated in transcriptional repression through deacetylation of acetyllysines in amino-terminal tails of core histones. In an immunoaffinity purification using anti-HDAC3, transcription factor TFII-I copurified with HDAC3. Specificity of the HDAC3-TFII-I interaction was confirmed by coimmunoprecipitation of epitope-tagged proteins, GST pull-down assays, and protein colocalization with indirect immunofluorescence. An anti-TFII-I immunoprecipitate contained histone deacetylase enzymatic activity. Mutational analyses revealed that the carboxyl-terminal of HDAC3 (residues 373-401) and residues 363-606 of TFII-I were required for the HDAC3-TFII-I interaction. Transcriptional activation by TFII-I was severely reduced by overexpression of HDAC3. These results suggest that HDAC3 modulates some of the functions of TFII-I and provides a link between histone deacetylase and a multifunctional transcriptional activator.

* This work was supported by National Institutes of Health Grants GM58486 (to E. S.) and AI45150 (to A. L. R.).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.

To whom correspondence should be addressed: Interdisciplinary Oncology Program, H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, 12902 Magnolia Dr., Tampa, FL 33612. Tel.: 813-979-6754; Fax: 813-979-7264; E-mail: setoe@moffitt.usf.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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