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Poly(ADP-ribose) Binds to Specific Domains of p53 and Alters Its DNA Binding Functions
Open accessAbstract
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.
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Citations
Cited by
The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
Ray Chaudhuri, A., & Nussenzweig, A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.53 · Cited by 1,786
The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors
Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373
p53 and Human Cancer: The First Ten Thousand Mutations
(1999) · Advances in Cancer Research · doi:10.1016/s0065-230x(08)60785-x · Cited by 986
Age related changes in NAD+ metabolism oxidative stress and Sirt1 activity in wistar rats
Braidy, N., Guillemin, G. J., Mansour, H., Chan-Ling, T., Poljak, A., & Grant, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019194 · Cited by 594
RetractedHassa, P. (2008) · Frontiers in Bioscience · doi:10.2741/2909 · Cited by 584
Metadata
- Authors
- Malanga, M., Pleschke, J. M., Kleczkowska, H. E., & Althaus, F. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-05
- Volume
- 273
- Issue
- 19
- Pages
- 11839-11843
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2032205501
- Cited by
- 220
- References
- 0
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Poly(ADP-ribose) Binds to Specific Domains of p53 and Alters Its DNA Binding Functions. https://app.cochat.ai/papers/10.1074/jbc.273.19.11839
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- Malanga, M., Pleschke, J. M., Kleczkowska, H. E., & Althaus, F. R. (1998). Poly(ADP-ribose) Binds to Specific Domains of p53 and Alters Its DNA Binding Functions. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.19.11839
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