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Originally published In Press as doi:10.1074/jbc.M003956200 on June 28, 2000

J. Biol. Chem., Vol. 275, Issue 39, 30478-30486, September 29, 2000
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Rapid Dephosphorylation of H1 Histones after Apoptosis Induction*

Martin KratzmeierDagger , Werner Albig, Kristina Hänecke, and Detlef Doenecke§

From the Institute for Biochemistry and Molecular Cell Biology, University of Göttingen, Humboldtallee 23, 37073 Göttingen, Germany

H1 histones are involved in the formation of higher order chromatin structures and in the modulation of gene expression. Changes in chromatin structure are a characteristic initial feature of apoptosis. We therefore have investigated the histone H1 pattern of the human leukemic cell line HL60 undergoing programmed cell death, as induced by topoisomerase I inhibition. Histone H1 proteins were isolated and analyzed by high performance liquid chromatography and capillary zone electrophoresis. DNA fragmentation after apoptosis induction was monitored by agarose gel electrophoresis. The patterns of the three H1 histone subtypes extractable from apoptotic HL60 cells significantly differed from those of control cells in showing a decrease of phosphorylated H1 subtypes and an increase of the respective dephosphorylated forms. This dephosphorylation of H1 histones could be observed already 45 min after apoptosis induction and preceded internucleosomal DNA cleavage by approximately 2 h. We conclude that during apoptotic DNA fragmentation, the H1 histones become rapidly dephosphorylated by a yet unknown protein phosphatase.

* This work was supported by the Deutsche Forschungsgemeinschaft (DFG) Grants SFB500 and Do 143/19-1 and the Fonds der Chemischen Industrie.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.

Dagger Present address: Agilent Technologies GmbH, Hewlett-Packard-Str. 8, 76337 Waldbronn, Germany.

§ To whom correspondence and reprint requests should be addressed: Tel.: 49-551-395972; Fax: 49-551-395960; E-mail: ddoenec@gwdg.de.

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