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Originally published In Press as doi:10.1074/jbc.M112037200 on May 6, 2002

J. Biol. Chem., Vol. 277, Issue 29, 26673-26680, July 19, 2002
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DNA Ligase III Is Degraded by Calpain during Cell Death Induced by DNA-damaging Agents*

Laura BordoneDagger and Colin Campbell§

From the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455

A yeast two-hybrid screen identified the regulatory subunit of the calcium-dependent protease calpain as a putative DNA ligase III-binding protein. Calpain binds to the N-terminal region of DNA ligase III, which contains an acidic proline, aspartate, serine, and threonine (PEST) domain frequently present in proteins cleaved by calpain. Recombinant DNA ligase III was a substrate for calpain degradation in vitro. This calpain-mediated proteolysis was calcium-dependent and was blocked by the specific calpain inhibitor calpeptin. Western blot analysis revealed that DNA ligase III was degraded in human fibrosarcoma HT1080 cells following exposure to gamma -radiation. The degradation of DNA ligase III was prevented by pretreatment with calpeptin, which protected irradiated cells from death. Calpeptin treatment also blocked 9-amino camptothecin-induced DNA ligase III proteolysis and simultaneously protected the cells from death. HT1080 clones expressing a modified DNA ligase III that lacked a recognizable PEST domain were significantly more resistant to killing by gamma -radiation or 9- amino camptothecin than were cells that overexpressed the wild-type form of DNA ligase III. These data show that calpain-mediated proteolysis of DNA ligase III plays an essential role in DNA damage-induced cell death in human cells.

* This work was supported in part by National Institutes of Health Grants CA61906 and AG16678 and the American Heart Association.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 Supported by American Heart Association Northland Affiliate Predoctoral Fellowship 9951198Z.

§ To whom correspondence should be addressed: Dept. of Pharmacology, University of Minnesota Medical School, 6-120 Jackson Hall, 321 Church St., SE, Minneapolis, MN 55455. Tel.: 612-625-8986; Fax: 612-625-8408; E-mail: campb034@umn.edu.

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