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Originally published In Press as doi:10.1074/jbc.M106528200 on October 4, 2001

J. Biol. Chem., Vol. 276, Issue 49, 45588-45597, December 7, 2001
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The Enzymatic and DNA Binding Activity of PARP-1 Are Not Required for NF-kappa B Coactivator Function*

Paul O. Hassa, Marcela Covic, Sameez Hasan, Ralph Imhof, and Michael O. HottigerDagger

From the Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland

Poly(ADP-ribose) polymerase 1 (PARP-1)-deficient mice are protected against septic shock, diabetes type I, stroke, and inflammation. We report that primary cells from PARP-1-/- animals are impaired in kappa B-dependent transcriptional activation induced by different stimuli involved in inflammatory and genotoxic stress signaling. PARP-1 was also required for p65-mediated transcriptional activation. PARP-1 enzymatic inhibitors did not inhibit the transcriptional activation of a kappa B-dependent reporter gene in wild type cells. Remarkably, neither the enzymatic activity nor the DNA binding activity of PARP-1 was required for kappa B-dependent transcriptional activation in PARP-1-/- cells complemented with different PARP-1 mutants. However, PARP-1 interacted in vitro directly with both subunits of NF-kappa B (p50 and p65), and mapping of the interaction domains revealed that both subunits bind to different PARP-1 domains. Furthermore, a PARP-1 mutant lacking the enzymatic and DNA binding activity interacted comparably to the wild type PARP-1 with p65 or p50. Finally, we showed that PARP-1 is activating the natural inducible nitric-oxide synthase and P-selectin promoter in a kappa B-dependent manner upon stimulation of the cells with inflammatory stimuli or cotransfection of p65. Our results provide evidence that neither the DNA binding nor the enzymatic activity of PARP-1 but its direct protein-protein interaction with both subunits of NF-kappa B is required for its coactivator function, thus expanding the role of PARP-1 as an essential and novel classical transcriptional coactivator for kappa B-dependent gene expression in vivo.

* This work was supported in part by Novartis as part of the ZNZ/Novartis Research Collaboration, by the EMDO Foundation (to M. C.), and Swiss National Science Foundation Grant 3100-57285.99 (to P. O. H. and S. H.).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 the Kanton of Zurich. To whom correspondence should be addressed. Tel.: 41-1-635-54-74; Fax: 41-1-635-68-40; E-mail: hottiger@vetbio.unizh.ch.

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