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Papers In Press, published online ahead of print October 2, 2000
J. Biol. Chem, 10.1074/jbc.M006520200
Submitted on July 21, 2000
Revised on September 18, 2000
Accepted on October 2, 2000

Poly(ADP-ribose) binds to specific domains in DNA checkpoint proteins

Jutta M. Pleschke, Hanna E. Kleczkowska, Mark Strohm, and Felix R. Althaus

Pharmacology and Toxicology, University of Zurich-Tierspital, Zurich, ZH CH-8057

Corresponding Author: fra{at}vetpharm.unizh.ch

Poly(ADP-ribose) is formed in possibly all multicellular organisms by a familiy of poly(ADP-ribose) polymerases (PARPs1). PARP-1, the best understood and until recently the only known member of this family, is a DNA damage signal protein catalyzing its automodification with multiple, variably sized ADP-ribose polymers that may contain up to 200 residues and several branching points. Through these polymers, PARP-1 can interact noncovalently with other proteins and alter their functions. Here we report the discovery of a poly(ADP-ribose)-binding sequence motif in several important DNA damage checkpoint proteins. The 20 amino acid motif contains two conserved regions: i) a cluster rich in basic amino acids and ii) a pattern of hydrophobic amino acids interspersed with basic residues. Using a combination of alanine scanning, polymer blot analysis and photoaffinity labeling, we have identified poly(ADP-ribose)-binding sites in the following proteins: p53, p21CIP1/WAF1, XPA, MSH6, DNA ligase III, XRCC1, DNA polymerase e, DNA-PKCS, Ku70, NF-kB, iNOS, CAD and telomerase. The poly(ADP-ribose)-binding motif was found to overlap with five important functional domains responsible for i) protein-protein interactions, ii) DNA-binding, iii) nuclear localization, iv) nuclear export, and v) protein degradation. Thus, PARPs may target specific signal network proteins via poly(ADP-ribose) and regulate their domain functions.


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