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Originally published In Press as doi:10.1074/jbc.M100290200 on July 30, 2001

J. Biol. Chem., Vol. 276, Issue 41, 38307-38319, October 12, 2001
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Regulation of Global Acetylation in Mitosis through Loss of Histone Acetyltransferases and Deacetylases from Chromatin*

Michael J. KruhlakDagger , Michael J. HendzelDagger §, Wolfgang Fischle||, Nicholas R. Bertos**, Shahid HameedDagger , Xiang-Jiao Yang**, Eric Verdin, and David P. Bazett-JonesDagger Dagger Dagger

From the Dagger  Research Institute, The Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada, the  Gladstone Institute for Virology and Immunology, University of California, San Francisco, California 94103, and the ** Molecular Oncology Group, Department of Medicine, McGill University Health Centre, Montreal, Quebec H3A 1A1, Canada

Histone acetylation, a reversible modification of the core histones, is widely accepted to be involved in remodeling chromatin organization for genetic reprogramming. Histone acetylation is a dynamic process that is regulated by two classes of enzymes, the histone acetyltransferases (HATs) and histone deacetylases (HDACs). Although promoter-specific acetylation and deacetylation has received most of the recent attention, it is superimposed upon a broader acting and dynamic acetylation that profoundly affects many nuclear processes. In this study, we monitored this broader histone acetylation as cells enter and exit mitosis. In contrast to the hypothesis that HATs and HDACs remain bound to mitotic chromosomes to provide an epigenetic imprint for postmitotic reactivation of the genome, we observed that HATs and HDACs are spatially reorganized and displaced from condensing chromosomes as cells progress through mitosis. During mitosis, HATs and HDACs are unable to acetylate or deacetylate chromatin in situ despite remaining fully catalytically active when isolated from mitotic cells and assayed in vitro. Our results demonstrate that HATs and HDACs do not stably bind to the genome to function as an epigenetic mechanism of selective postmitotic gene activation. Our results, however, do support a role for spatial organization of these enzymes within the cell nucleus and their relationship to euchromatin and heterochromatin postmitotically in the reactivation of the genome.

* This project was funded by operating grants from the Canadian Institutes of Health Research (to D. P. B.-J. and X.-J. Y.).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.

§ Supported by studentships from University Technologies International (University of Calgary), Alberta Heritage Foundation for Medical Research, and the Alberta Cancer Board. Present address: Dept. of Oncology, Cross Cancer Institute, University of Alberta, Edmonton, Alberta T6G 1Z2, Canada.

|| Supported by the Boehringer Ingelheim Foundation (Germany).

Dagger Dagger To whom correspondence should be addressed: Dr. David P. Bazett-Jones, Research Institute, The Hospital for Sick Children, 555 Univ. Ave., Toronto, ON M5G 1X8, Canada. Tel.: 416-813-2181; Fax: 416-813-5028; E-mail: dbjones@sickkids.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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