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J Biol Chem, Vol. 273, Issue 19, 11839-11843, May 8, 1998
From the Institute of Pharmacology and Toxicology, University of
Zürich-Tierspital, Winterthurerstrasse 260, CH-8057 Zürich, Switzerland
DNA strand breaks are potential interaction sites
for the nuclear enzyme poly(ADP-ribose) polymerase (PARP; E.C.
2.4.2.30) and the tumor suppressor protein p53. Both proteins bind and
respond to DNA breaks and both play a role in DNA damage signaling. A temporary colocalization and complex formation between these proteins has been demonstrated in mammalian cells. Here we show that free and
poly(ADP-ribose) polymerase-bound ADP-ribose polymers target three
domains in p53 protein for strong noncovalent interactions. The polymer
binding sites could be mapped to two amino acid sequences in the
sequence-specific core DNA binding domain of p53 (amino acid positions
153-178 and 231-253) and another one in the oligomerization domain
(amino acids 326-348). In mobility shift experiments, poly(ADP-ribose) effectively prevented and reversed p53 binding to the palindromic p53
consensus sequence. Additionally, poly(ADP-ribose) also interfered with
the DNA single strand end binding of p53. The results suggest that
ADP-ribose polymers could play a role in regulating the DNA binding
properties of p53.
Poly(ADP-ribose) Binds to Specific Domains of p53 and Alters Its
DNA Binding Functions
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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