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Originally published In Press as doi:10.1074/jbc.M201027200 on April 1, 2002

J. Biol. Chem., Vol. 277, Issue 24, 21683-21690, June 14, 2002
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Modeling Apoptotic Chromatin Condensation in Normal Cell Nuclei
REQUIREMENT FOR INTRANUCLEAR MOBILITY AND ACTIN INVOLVEMENT*

Piotr WidlakDagger , Olena PalyvodaDagger , Slawomir KumalaDagger , and William T. Garrard§

From the Dagger  Department of Experimental and Clinical Radiobiology, Center of Oncology, 44-100 Gliwice, Poland and the § Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390

Hallmarks of the terminal stages of apoptosis are genomic DNA fragmentation and chromatin condensation. Here, we have studied the mechanism of condensation both in vitro and in vivo. We found that DNA fragmentation per se of isolated nuclei from non-apoptotic cells induced chromatin condensation that closely resembles the morphology seen in apoptotic cells, independent of ATP utilization, at physiological ionic strengths. Interestingly, chromatin condensation was accompanied by release of nuclear actin, and both condensation and actin release could be blocked by reversibly pretreating nuclei with Ca2+, Cu2+, diamide, or low pH, procedures shown to stabilize internal nuclear components. Moreover, specific inhibition of nuclear F-actin depolymerization or promotion of its formation also reduced chromatin condensation. Chromatin condensation could also be inhibited by exposing nuclei to reagents that bind to the DNA minor groove, disrupting native nucleosomal DNA wrapping. In addition, in cultured cells undergoing apoptosis, drugs that inhibit depolymerization of actin or bind to the minor groove also reduced chromatin condensation, but not DNA fragmentation. Therefore, the ability of chromatin fragments with intact nucleosomes to form large clumps of condensed chromatin during apoptosis requires the apparent disassembly of internal nuclear structures that may normally constrain chromosome subdomains in non-apoptotic cells.

* This work was supported in part by Grant 6P04A01317 from the Polish Committee for Scientific Research KBN (to P. W.), Grant GMRO1-59809 from the National Institutes of Health, and Grant I-0823 from the Robert A. Welch Foundation (to W. T. G.).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 and reprint requests should be addressed: Dept. of Molecular Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9148. Tel.: 214-648-1924; Fax: 214-648-1915; E-mail: william.garrard@utsouthwestern.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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