PARP2

This gene encodes poly(ADP-ribosyl)transferase-like 2 protein, which contains a catalytic domain and is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. The basic residues within the N-terminal region of this protein may bear potential DNA-binding properties, and may be involved in the nuclear and/or nucleolar targeting of the protein. Two alternatively spliced transcript variants encoding distinct isoforms have been found.

In the plant species Arabidopsis thaliana, PARP2 plays more significant roles than PARP1 in protective responses to DNA damage and bacterial pathogenesis.{{cite journal | vauthors = Song J, Keppler BD, Wise RR, Bent AF | title = PARP2 Is the Predominant Poly(ADP-Ribose) Polymerase in Arabidopsis DNA Damage and Immune Responses | journal = PLOS Genetics | volume = 11 | issue = 5 | pages = e1005200 | date = May 2015 | pmid = 25950582 | pmc = 4423837 | doi = 10.1371/journal.pgen.1005200 | doi-access = free }} The plant PARP2 carries N-terminal SAP DNA binding motifs rather than the Zn-finger DNA binding motifs of plant and animal PARP1 proteins.

Some PARP inhibitor anti-cancer drugs (primarily aimed at PARP1) also inhibit PARP2, e.g. niraparib.

PARP2 has been shown to interact with XRCC1.{{cite journal | vauthors = Schreiber V, Amé JC, Dollé P, Schultz I, Rinaldi B, Fraulob V, Ménissier-de Murcia J, de Murcia G | title = Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 25 | pages = 23028–36 | date = June 2002 | pmid = 11948190 | doi = 10.1074/jbc.M202390200 | doi-access = free }}

PARP2 also interacts with HPF1.{{cite journal | vauthors = Gibbs-Seymour I, Fontana P, Rack JG, Ahel I | title =

HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity | journal = Molecular Cell | volume = 62 | issue = 3 | pages = 432–442 | date = 5 May 2016 | pmid = 27067600 | doi = 10.1016/j.molcel.2016.03.008 | pmc = 4858568 }}{{cite journal | vauthors = Suskiewicz MJ, Zobel F, Ogden TE, Fontana P, Ariza A, Yang JC, Zhu K, Bracken L, Hawthorne WJ, Ahel D, Neuhaus D, Ahel I | title = HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation | journal = Nature | volume = 579 | issue = 7800 | pages = 598–602 | date = March 2020 | pmid = 32028527 | doi = 10.1038/s41586-020-2013-6 | pmc = 7104379 | bibcode = 2020Natur.579..598S }}{{cite journal | vauthors = Gaullier G, Roberts G, Muthurajan UM, Bowerman S, Rudolph J, Mahadevan J, Jha A, Rae PS, Luger K | title = Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1 | journal = PLOS ONE | volume = 15 | issue = 11 | pages = e0240932 | date = 3 November 2020 | pmid = 33141820 | doi = 10.1371/journal.pone.0240932 | pmc = 7608914 | bibcode = 2020PLoSO..1540932G | doi-access = free }}

PARP2 binds to and bridges blunt DNA ends.{{cite journal | vauthors = Obaji E, Haikarainen T, Lehtiö L | title = Structural basis for DNA break recognition by ARTD2/PARP2 | journal = Nucleic Acids Research | volume = 46 | issue = 22 | pages = 12154–12165 | date = 14 December 2018 | pmid = 30321391 | doi = 10.1093/nar/gky927 | pmc = 6294510 }}{{cite journal | vauthors = Bilokapic S, Suskiewicz MJ, Ahel I, Halic M | title = Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin | journal = Nature | volume = 585 | issue = 7826 | pages = 609–613 | date = September 2020 | pmid = 32939087 | doi = 10.1038/s41586-020-2725-7 | pmc = 7529888 | bibcode = 2020Natur.585..609B }}

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• {{cite journal | vauthors = Bashford CL, Chance B, Lloyd D, Poole RK | title = Oscillations of redox states in synchronously dividing cultures of Acanthamoeba castellanii and Schizosaccharomyces pombe | journal = Biophysical Journal | volume = 29 | issue = 1 | pages = 1–11 | date = January 1980 | pmid = 7260241 | pmc = 1328658 | doi = 10.1016/S0006-3495(80)85114-9 | bibcode = 1980BpJ....29....1B }}
• {{cite journal | vauthors = Berghammer H, Ebner M, Marksteiner R, Auer B | title = pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans | journal = FEBS Letters | volume = 449 | issue = 2–3 | pages = 259–63 | date = April 1999 | pmid = 10338144 | doi = 10.1016/S0014-5793(99)00448-2 | doi-access = free }}
• {{cite journal | vauthors = Amé JC, Rolli V, Schreiber V, Niedergang C, Apiou F, Decker P, Muller S, Höger T, Ménissier-de Murcia J, de Murcia G | title = PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase | journal = The Journal of Biological Chemistry | volume = 274 | issue = 25 | pages = 17860–8 | date = June 1999 | pmid = 10364231 | doi = 10.1074/jbc.274.25.17860 | doi-access = free }}
• {{cite journal | vauthors = Still IH, Vince P, Cowell JK | title = Identification of a novel gene (ADPRTL1) encoding a potential Poly(ADP-ribosyl)transferase protein | journal = Genomics | volume = 62 | issue = 3 | pages = 533–6 | date = December 1999 | pmid = 10644454 | doi = 10.1006/geno.1999.6024 }}
• {{cite journal | vauthors = Schreiber V, Amé JC, Dollé P, Schultz I, Rinaldi B, Fraulob V, Ménissier-de Murcia J, de Murcia G | title = Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 25 | pages = 23028–36 | date = June 2002 | pmid = 11948190 | doi = 10.1074/jbc.M202390200 | doi-access = free }}
• {{cite journal | vauthors = Saxena A, Wong LH, Kalitsis P, Earle E, Shaffer LG, Choo KH | title = Poly(ADP-ribose) polymerase 2 localizes to mammalian active centromeres and interacts with PARP-1, Cenpa, Cenpb and Bub3, but not Cenpc | journal = Human Molecular Genetics | volume = 11 | issue = 19 | pages = 2319–29 | date = September 2002 | pmid = 12217960 | doi = 10.1093/hmg/11.19.2319 | doi-access = free }}
• {{cite journal | vauthors = Malanga M, Althaus FR | title = Poly(ADP-ribose) reactivates stalled DNA topoisomerase I and Induces DNA strand break resealing | journal = The Journal of Biological Chemistry | volume = 279 | issue = 7 | pages = 5244–8 | date = February 2004 | pmid = 14699148 | doi = 10.1074/jbc.C300437200 | doi-access = free }}
• {{cite journal | vauthors = Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Research | volume = 16 | issue = 1 | pages = 55–65 | date = January 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
• {{cite journal | vauthors = Maeda Y, Hunter TC, Loudy DE, Davé V, Schreiber V, Whitsett JA | title = PARP-2 interacts with TTF-1 and regulates expression of surfactant protein-B | journal = The Journal of Biological Chemistry | volume = 281 | issue = 14 | pages = 9600–6 | date = April 2006 | pmid = 16461352 | doi = 10.1074/jbc.M510435200 | doi-access = free }}
• {{cite journal | vauthors = Chevanne M, Calia C, Zampieri M, Cecchinelli B, Caldini R, Monti D, Bucci L, Franceschi C, Caiafa P | title = Oxidative DNA damage repair and parp 1 and parp 2 expression in Epstein-Barr virus-immortalized B lymphocyte cells from young subjects, old subjects, and centenarians | journal = Rejuvenation Research | volume = 10 | issue = 2 | pages = 191–204 | date = June 2007 | pmid = 17518695 | doi = 10.1089/rej.2006.0514 }}
• {{cite journal | vauthors = Liang YC, Hsu CY, Yao YL, Yang WM | title = PARP-2 regulates cell cycle-related genes through histone deacetylation and methylation independently of poly(ADP-ribosyl)ation | journal = Biochemical and Biophysical Research Communications | volume = 431 | issue = 1 | pages = 58–64 | date = February 2013 | pmid = 23291187 | doi = 10.1016/j.bbrc.2012.12.092 }}
• {{cite journal | vauthors = Song J, Keppler BD, Wise RR, Bent AF | title = PARP2 Is the Predominant Poly(ADP-Ribose) Polymerase in Arabidopsis DNA Damage and Immune Responses | journal = PLOS Genetics | volume = 11 | issue = 5 | pages = e1005200 | date = May 2015 | pmid = 25950582 | pmc = 4423837 | doi = 10.1371/journal.pgen.1005200 | doi-access = free }}

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• {{UCSC genome browser|PARP2}}
• {{UCSC gene details|PARP2}}

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