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Papers In Press, published online ahead of print October 4, 2001
J. Biol. Chem, 10.1074/jbc.M106528200
Submitted on July 12, 2001
Revised on October 4, 2001
Accepted on October 4, 2001

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. Hottiger

Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Zurich 8057

Corresponding Author: hottiger{at}vetbio.unizh.ch

Poly (ADP-Ribose) Polymerase 1 (PARP-1) deficient mice are protected against septic shock, diabetes type I, stroke and inflammation. Here we report that primary cells from PARP-1-/- animals are impaired in kB-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 kB-dependent reporter gene in wild type cells. Remarkably neither the enzymatic activity nor the DNA binding activity of PARP-1 were required for kB-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-kB (p50 and p65) and mapping of the interaction domains revealed that both subunits bind to different PARP-1 domains. Furthermore, PARP-1 mutant lacking the enzymatic and DNA binding activity interacted comparable to the wild type PARP-1 with p65 or p50. Finally, we showed that PARP-1 is activating the natural iNOS and P-Selectin promoter in a kB-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-kB is required for its coactivator function, thus expanding the role of PARP-1 as an essential and novel classical transcriptional coactivator for kB-dependent gene expression in vivo.


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