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Originally published In Press as doi:10.1074/jbc.M008044200 on December 20, 2000

J. Biol. Chem., Vol. 276, Issue 14, 11279-11286, April 6, 2001
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Functional Competition between Poly(ADP-ribose) Polymerase and Its 24-kDa Apoptotic Fragment in DNA Repair and Transcription*

Tetsu M. C. Yung and Masahiko S. SatohDagger

From the DNA Repair Group, Health and Environment Unit, Laval University Medical Centre, CHUQ, Faculty of Medicine, Laval University, Ste-Foy, Quebec G1V 4G2, Canada

Poly(ADP-ribose) polymerase is a 113-kDa nuclear enzyme that binds to both damaged DNA and to RNA associated with actively transcribed regions of chromatin. Binding of poly(ADP-ribose) polymerase to DNA lesions activates it, catalyzing the covalent addition of multiple ADP-ribose polymers to the enzyme (automodification). During apoptosis, poly(ADP-ribose) polymerase is cleaved by caspase-3, resulting in the formation of an N-terminal 24-kDa fragment, containing the DNA binding domain, and a C-terminal 89-kDa catalytic fragment. The functional relevance of this cleavage is not well understood. We therefore prepared a recombinant 24-kDa poly(ADP-ribose) polymerase fragment and investigated the role of this fragment in DNA repair and transcription. The 24-kDa fragment retained its binding affinity for both DNA breaks and RNA. In an in vitro cell-free DNA repair assay, this fragment inhibited rejoining of DNA breaks and suppressed ADP-ribose polymer formation by competing with poly(ADP-ribose) polymerase in binding to DNA breaks. With regard to transcription, it has recently been demonstrated that binding of poly(ADP-ribose) polymerase to transcribed RNA reduces the rate of transcript elongation and that automodification of poly(ADP-ribose) polymerase bound to DNA breaks results in up-regulation of transcription. We tested the 24-kDa fragment for its ability to suppress transcript elongation, and we found that it competed against the up-regulation of transcription mediated by full-length poly(ADP-ribose) polymerase. The ability of the 24-kDa fragment to inhibit DNA repair, ADP-ribose polymer formation, and damage-dependent up-regulation of transcription may contribute to the apoptotic shift from cell survival to cell death mode.

* This work was supported in part by the National Cancer Institute of Canada for the Terry Fox Run and the Canadian Institutes of Health Research; The Canada Foundation for Innovation and the Quebec government provided infrastructure support.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 a salary support award from the Canadian Institutes of Health Research. To whom correspondence should be addressed: DNA Repair Group, Health and Environment Unit, Laval University Medical Centre, CHUQ, Faculty of Medicine, Laval University, 2705 Blvd. Laurier, Ste-Foy, Quebec G1V 4G2, Canada. Tel.: 418-656-4141 (Ext. 7340); Fax: 418-654-2159; E-mail: Masahiko.sato@crchul.ulaval.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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