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J Biol Chem, Vol. 274, Issue 26, 18715-18720, June 25, 1999

Histone H1 Dephosphorylation Is Mediated through a Radiation-induced Signal Transduction Pathway Dependent on ATM

Chang Y. GuoDagger , Yu WangDagger , David L. Brautigan§, and James M. LarnerDagger

From the Dagger  Department of Radiation Oncology, University of Virginia Health Science System, Charlottesville, Virginia 22908 and the § Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908

Ionizing radiation is known to activate multiple signal transduction pathways, but the targets of these pathways are poorly understood. Phosphorylation of histone H1 is thought to have a role in chromatin condensation/decondensation, and we asked whether ionizing radiation (IR) would alter H1 phosphorylation. Our data demonstrate that low doses of IR result in a dramatic, but transient, dephosphorylation of H1 isoforms. The in vivo IR-induced dephosphorylation of H1 is completely blocked by wortmannin and is abrogated in ataxia telangiectasia cells. Furthermore, we measured radiation-induced inhibition of cyclin dependent kinase activity and activation of histone H1 phosphatase activity. Both activities were affected by radiation-induced signals in an ATM-dependent manner. Thus, the rapid IR-induced dephosphorylation of H1 involves a pathway including ATM and a wortmannin-sensitive step leading to both inhibition of cyclin-dependent kinase activities as well as activation of H1 phosphatase(s).

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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