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J. Biol. Chem., Vol. 275, Issue 52, 40974-40980, December 29, 2000
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From the Institute of Pharmacology and Toxicology, University of
Zurich, Tierspital, Winterthurerstrasse 260, CH-8057 Zurich, Switzerland
Poly(ADP-ribose) is formed in possibly all
multicellular organisms by a familiy of poly(ADP-ribose)
polymerases (PARPs). 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, xeroderma pigmentosum group A
complementing protein, MSH6, DNA ligase III, XRCC1, DNA polymerase
Poly(ADP-ribose) Binds to Specific Domains in DNA Damage
Checkpoint Proteins*
,
,
DNA-PKCS, Ku70, NF-
B, inducible nitric-oxide synthase,
caspase-activated DNase, 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.
*
This work was supported by grants (to F. R. A.)
from the Swiss National Foundation for Scientific Research and the
Swiss Federal Office for Public Health.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.
On leave from the Inst. of Nuclear Chemistry and Technology, PL-03
195 Warsaw, Poland.
§
To whom correspondence should be addressed. Tel.: 411-635-87-62;
Fax: 411-635-89-10; E-mail: fra@vetpharm.unizh.ch.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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