Poly(ADP-ribose) Contributes to an Association between Poly(ADP-ribose) Polymerase-1 and Xeroderma Pigmentosum Complementation Group A in Nucleotide Excision Repair

King, Brenee; Cooper, Karen L.; Liu, Ke Jian; Hudson, Laurie G.

doi:10.1074/jbc.m112.393504

Cited by 60 publications

(61 citation statements)

References 42 publications

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“…The findings are in agreement with those obtained by other groups (Litwin et al, 2013;Qin et al, 2012). There is also evidence showing that PARP contributes to XPA repair of double strand breaks (King et al, 2012). As þ3 has been documented to interact with other environmental agents, such as UVR (Cooper et al, 2009(Cooper et al, , 2013Evans et al, 2004;Zhou et al, 2011).…”

Section: Introductionsupporting

confidence: 82%

Editor’s Highlight: Interactive Genotoxicity Induced by Environmentally Relevant Concentrations of Benzo(a)Pyrene Metabolites and Arsenite in Mouse Thymus Cells

Lauer

Liu

et al. 2016

Toxicol. Sci.

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Arsenic and polycyclic aromatic hydrocarbon (PAH) exposures affect many people worldwide leading to cancer and other diseases. Arsenite (As þ3 ) and certain PAHs are known to cause genotoxicity. However, there is limited information on the interactions between As þ3 and PAHs at environmentally relevant concentrations. The thymus is the primary immune organ for T cell development in mammals. Our previous studies showed that environmentally relevant concentrations of As þ3 induce genotoxicity in mouse thymus cells through Poly(ADP-ribose) polymerase (PARP) inhibition. Certain PAHs, such as the metabolites of benzo(a)pyrene (BaP), are known to cause DNA damage by forming DNA adducts. In the present study, primary mouse thymus cells were examined for DNA damage following 18 hr in vitro treatments with 5 or 50 nM As þ3 and 100 nM BaP, benzo[a]pyrene-7,8-dihydrodiol (BP-Diol), or benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide (BPDE). An interactive increase in genotoxicity and apoptosis were observed following treatments with 5 nM As þ 3 þ 100 nM BP-diol and 50 nM As þ 3 þ 100 nM BPDE. We attribute the increase in DNA damage to inhibition of PARP inhibition leading to decreased DNA repair. To further support this hypothesis, we found that a PARP inhibitor, 3,4-dihydro-5[4-(1-piperindinyl) butoxyl]-1(2H)-isoquinoline (DPQ), also interacted with BP-diol to produce an increase in DNA damage. Interestingly, we also found that As þ3 and BP-diol increased CYP1A1 and CYP1B1 expression, suggesting that increased PAH metabolism may also contribute to genotoxicity. In summary, these results show that the suppression of PARP activity and induction of CYP1A1/ CYP1B1 may act together to increase DNA damage produced by As þ3 and PAHs.

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Section: Introductionsupporting

confidence: 82%

Editor’s Highlight: Interactive Genotoxicity Induced by Environmentally Relevant Concentrations of Benzo(a)Pyrene Metabolites and Arsenite in Mouse Thymus Cells

Lauer

Liu

et al. 2016

Toxicol. Sci.

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“…1a, right panel). Next, we tried previously described formaldehyde-Triton protocol 8 which was shown to display a punctate pattern of PARP-1. However, we noted that this pattern did not correlate with recruitment of PARP-1 to UV-damaged DNA, because it was observed in both the unirradiated control and globally UVC-irradiated cells; and none of the spots of PARP-1 were co-incident with DDB2, i.e., UV-damaged DNA in the cells after local UVC-irradiation ( Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

Characterization of the interactions of PARP-1 with UV-damaged DNA in vivo and in vitro

Purohit

Robu

Shah

et al. 2016

Sci Rep

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The existing methodologies for studying robust responses of poly (ADP-ribose) polymerase-1 (PARP-1) to DNA damage with strand breaks are often not suitable for examining its subtle responses to altered DNA without strand breaks, such as UV-damaged DNA. Here we describe two novel assays with which we characterized the interaction of PARP-1 with UV-damaged DNA in vivo and in vitro. Using an in situ fractionation technique to selectively remove free PARP-1 while retaining the DNA-bound PARP-1, we demonstrate a direct recruitment of the endogenous or exogenous PARP-1 to the UV-lesion site in vivo after local irradiation. In addition, using the model oligonucleotides with single UV lesion surrounded by multiple restriction enzyme sites, we demonstrate in vitro that DDB2 and PARP-1 can simultaneously bind to UV-damaged DNA and that PARP-1 casts a bilateral asymmetric footprint from −12 to +9 nucleotides on either side of the UV-lesion. These techniques will permit characterization of different roles of PARP-1 in the repair of UV-damaged DNA and also allow the study of normal housekeeping roles of PARP-1 with undamaged DNA.The abundance of poly (ADP-ribose) polymerase-1 (PARP-1) in mammalian cells and its rapid catalytic activation to form polymers of ADP-ribose (PAR) in the presence of various types of DNA damages with or without strand breaks has made it an ideal first responder at the lesion site to influence downstream events 1,2 . Apart from DNA damages, PARP-1 is also recruited to DNA during normal physiological processes such as transcription and chromatin remodeling 3 , which do not involve overt DNA damage but just altered DNA structures. While we know much more about how PARP-1 rapidly recognizes and binds to single or double strand breaks in DNA, we know very little about how PARP-1 interacts with DNA damages or altered DNA structures without strand breaks. The key reason is that the existing methodologies that readily identify interactions of PARP-1 with DNA strand breaks are not sufficiently sensitive to study the relatively weaker responses of PARP-1 to DNA damage without strand breaks. The response of PARP-1 to UVC-induced direct photolesions, such as cyclobutane pyrimidine dimers (CPD) that are formed without any DNA strand breaks exemplifies this problem.Recent studies from others and our team have shown the involvement of PARP-1 in the host cell reactivation 4 and specifically in the nucleotide excision repair (NER) of UV-damaged DNA through its interaction with early NER protein DDB2 [5][6][7] . Additional studies have shown that downstream NER proteins XPA 8,9 and XPC 10 are PARylated. Thus, PARP-1 possibly has multiple roles in NER, but we do not yet fully understand its interactions with UV-damaged DNA or other NER proteins due to two major challenges. The first challenge is that unlike for many NER proteins, the abundance of endogenous PARP-1 in the nucleus makes it nearly impossible to visualize its dynamics of recruitment to UV-damaged DNA in situ using conventional immunocytological methods. T...

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“…Thus, DNA damage-binding protein 2 (DDB2) that specifically recognizes UV-induced damages in DNA interacts with PARP1 and undergoes poly(ADP-ribosyl)ation (8,10). Another NER factor, xeroderma pigmentosum protein A also interacts with PARP1 and PAR (10,11). Moreover, PARP1 was identified as one of the main targets in HeLa cell extracts selectively labeled by a photoreactive DNA analogue of the NER substrate (12), suggesting the possible involvement of PARP1 in this repair process.…”

mentioning

confidence: 99%

“…In particular, data were reported on the involvement of PARP1 in chromatin decondensation at the sites of damage induced by UV irradiation and in the regulation of the interaction of the nucleotide excision repair (NER) factors with UV-damaged DNA (6 -10). Thus, DNA damage-binding protein 2 (DDB2) that specifically recognizes UV-induced damages in DNA interacts with PARP1 and undergoes poly(ADP-ribosyl)ation (8,10). Another NER factor, xeroderma pigmentosum protein A also interacts with PARP1 and PAR (10,11).…”

mentioning

confidence: 99%

Poly(ADP-ribose) Polymerase 1 Modulates Interaction of the Nucleotide Excision Repair Factor XPC-RAD23B with DNA via Poly(ADP-ribosyl)ation

Maltseva

Rechkunova

Sukhanova

et al. 2015

Journal of Biological Chemistry

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Background: Poly(ADP-ribosyl)ation of DNA repair proteins is essential for the regulation of DNA repair processes. Results: Both subunits of the nucleotide excision repair factor XPC-RAD23B are poly(ADP-ribosyl)ated by PARP1. Conclusion: PARP1 influences the interaction of XPC-RAD23B with DNA via PAR synthesis. Significance: This study provides direct evidence for XPC-RAD23B belonging to the targets of poly(ADP-ribosyl)ation catalyzed by PARP1.

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Poly(ADP-ribose) Contributes to an Association between Poly(ADP-ribose) Polymerase-1 and Xeroderma Pigmentosum Complementation Group A in Nucleotide Excision Repair

Cited by 60 publications

References 42 publications

Editor’s Highlight: Interactive Genotoxicity Induced by Environmentally Relevant Concentrations of Benzo(a)Pyrene Metabolites and Arsenite in Mouse Thymus Cells

Editor’s Highlight: Interactive Genotoxicity Induced by Environmentally Relevant Concentrations of Benzo(a)Pyrene Metabolites and Arsenite in Mouse Thymus Cells

Characterization of the interactions of PARP-1 with UV-damaged DNA in vivo and in vitro

Poly(ADP-ribose) Polymerase 1 Modulates Interaction of the Nucleotide Excision Repair Factor XPC-RAD23B with DNA via Poly(ADP-ribosyl)ation

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