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Volume 272, Number 16, Issue of April 18, 1997 pp. 10817-10822
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Condensation of Chromatin in Apoptotic Thymocytes Shows a Specific Structural Change

(Received for publication, October 18, 1996, and in revised form, February 4, 1997)

Caterina Allera ^§ , Giuseppe Lazzarini , Eligio Patrone , Ingles Alberti ^§ , Paola Barboro ^§ , Paola Sanna ^§ , Antonella Melchiori ^§ , Silvio Parodi ^§ and Cecilia Balbi ^§

From the  Istituto di Studi Chimico-Fisici di Macromolecole Sintetiche e Naturali, Via De Marini, 6 "Torre di Francia," 16146 Genoa, Italy and the ^§ Istituto Nazionale per la Ricerca sul Cancro, Largo Rosanna Benzi, 10, 16132 Genoa, Italy

Chromatin condensation and DNA cleavage at internucleosomal sites have been recognized early as hallmarks of apoptosis, and it has been suggested that extensive DNA chain scission could directly result in the formation of dense chromatin bodies. Here we have shown that no causal relationship exists between DNA degradation and chromatin condensation in glucocorticoid-induced thymocyte apoptosis. The chromatin rearrangement occurred independent of as well as prior to DNA cleavage and involved a specific conformational change at the nucleosome level. In the early stages of the process, the core particles appeared to be tightly packed face-to-face in smooth 11-nm filaments that progressively folded to generate a closely woven network. The network finally collapsed, producing dense apoptotic bodies. Since trypsin digestion relaxed condensed chromatin and histone H4 underwent appreciable deacetylation in the apoptotic cell, we suggest that changes in the DNA-histone interactions represented a major modulating factor of condensation.

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