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{{Short description|Mammalian protein found in Homo sapiens}}
{{Infobox_gene}}
'''Poly [ADP-ribose] polymerase 1''' ('''PARP-1''') also known as '''NAD<sup>+</sup> ADP-ribosyltransferase 1''' or '''poly[ADP-ribose] synthase 1''' is an [[enzyme]] that in humans is encoded by the ''PARP1'' [[gene]].<ref name="pmid10964595">{{cite journal | vauthors = Ha HC, Snyder SH | title = Poly(ADP-ribose) polymerase-1 in the nervous system | journal = [[Neurobiology of Disease]] | volume = 7 | issue = 4 | pages = 225–39 | date = August 2000 | pmid = 10964595 | doi = 10.1006/nbdi.2000.0324 | s2cid = 41201067 }}</ref> It is the most abundant of the [[Poly ADP ribose polymerase|PARP]] family of enzymes, accounting for 90% of the NAD+ used by the family.<ref name="pmid33028824">{{cite journal | vauthors=Xie N, Zhang L, Gao W, Huang C, Zou B | title=NAD + metabolism: pathophysiologic mechanisms and therapeutic potential | journal=[[Signal Transduction and Targeted Therapy]] | volume=5 | issue=1 | pages=227 | year=2020 | doi = 10.1038/s41392-020-00311-7 | pmc=7539288 | pmid=33028824}}</ref> PARP1 is mostly present in cell nucleus, but cytosolic fraction of this protein was also reported.<ref>{{cite journal |last1=Karpińska |first1=Aneta |title=Quantitative analysis of biochemical processes in living cells at a single-molecule level: a case of olaparib–PARP1 (DNA repair protein) interactions |journal=Analyst |year=2021 |volume=146 |issue=23 |pages=7131–7143 |doi=10.1039/D1AN01769A |pmid=34726203|bibcode=2021Ana...146.7131K |s2cid=240110114 |url=https://eprints.lancs.ac.uk/id/eprint/161906/1/AN_ART_09_2021_001769.R1_Proof_hi.pdf }}</ref>
== Function ==
PARP1 works:
* By using [[Nicotinamide adenine dinucleotide|NAD+]] to synthesize poly [[Adenosine diphosphate ribose|ADP ribose]] (PAR) and transferring PAR [[Moiety (chemistry)|moieties]] to proteins
* In conjunction with BRCA, which acts on double strands; members of the [[Poly ADP ribose polymerase|PARP]] family act on single strands; or, when BRCA fails, PARP takes over those jobs as well (in a DNA repair context).
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* Normal or abnormal recovery from DNA damage
* May be the site of mutation in [[Fanconi anemia]]{{Citation needed|date=January 2010}}
* Induction of inflammation.<ref name="pmid23050038">{{cite journal | vauthors=Mangerich A, Bürkle A | title=Pleiotropic cellular functions of PARP1 in longevity and aging: genome maintenance meets inflammation | journal=[[Oxidative Medicine and Cellular Longevity]] | volume=2012 | pages=321653 | year=2012 | doi = 10.1155/2012/321653 | pmc=3459245 | pmid=23050038| doi-access=free }}</ref>
* The pathophysiology of [[type I diabetes]].<ref name="entrez">{{cite web | title = Entrez Gene: PARP1 poly (ADP-ribose) polymerase family, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=142}}</ref>
PARP1 is activated by:
* [[Helicobacter pylori]] in the development and proliferation of [[gastric cancer]].<ref name="pmid19897724">{{cite journal | vauthors = Nossa CW, Jain P, Tamilselvam B, Gupta VR, Chen LF, Schreiber V, Desnoyers S, Blanke SR | display-authors = 6 | title = Activation of the abundant nuclear factor poly(ADP-ribose) polymerase-1 by Helicobacter pylori | journal = [[Proceedings of the National Academy of Sciences of the United States of America]] | volume = 106 | issue = 47 | pages = 19998–20003 | date = November 2009 | pmid = 19897724 | pmc = 2785281 | doi = 10.1073/pnas.0906753106 |
*{{cite web |date=January 6, 2010 |title=Team finds link between stomach-cancer bug and cancer-promoting factor |website=Medical Xpress |url=http://www.physorg.com/news182001373.html}}</ref>
=== Role in DNA damage repair ===
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=== Role in inflammation ===
PARP1 is required for [[NF-κB]] [[Transcription (biology)|transcription]] of [[Inflammation|proinflammatory]] mediators such as [[tumor necrosis factor]], [[interleukin 6]], and inducible [[nitric oxide synthase]].<ref name="pmid23050038" /><ref name="pmid28974953">{{cite journal | vauthors=Sethi GS, Dharwal V, Naura AS | title=Poly(ADP-Ribose)Polymerase-1 in Lung Inflammatory Disorders: A Review | journal=[[Frontiers in Immunology]] | volume=8 | pages=1172 | year=2017 | doi = 10.3389/fimmu.2017.01172 | pmc=5610677 | pmid=28974953| doi-access=free }}</ref> PARP1 activity contributes to the proinflammatory [[macrophage]]s that increase with age in many tissues.<ref name="pmid32774895">{{cite journal | vauthors=Yarbro JR, Emmons RS, Pence BD | title=Macrophage Immunometabolism and Inflammaging: Roles of Mitochondrial Dysfunction, Cellular Senescence, CD38, and NAD | journal=[[Immunometabolism (journal)|Immunometabolism]] | volume=2 | issue=3 | pages=e200026 | year=2020 | doi = 10.20900/immunometab20200026 | pmc=7409778 | pmid=32774895}}</ref> ADP-riboyslation of the [[HMGB1]] [[high-mobility group]] protein by PARP1 inhibits removal of [[apoptosis|apoptotic]] cells, thereby sustaining inflammation.<ref name="pmid31877876">{{cite journal | vauthors=Pazzaglia S, Pioli C | title=Multifaceted Role of PARP-1 in DNA Repair and Inflammation: Pathological and Therapeutic Implications in Cancer and Non-Cancer Diseases | journal=[[Cell (journal)|Cells]] | volume=9 | issue=1 | pages=41 | year=2019 | doi = 10.3390/cells9010041 | pmc=7017201 | pmid=31877876| doi-access=free }}</ref>
In [[asthma]] PARP1 facilitates recruitment and function of immune cells, including [[T helper cell|CD4+ T-cells]], [[eosinophil]]s, and [[dendritic cell]]s.<ref name="pmid28974953" />
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PARP1 is one of six enzymes required for the highly error-prone DNA repair pathway [[microhomology-mediated end joining]] (MMEJ).<ref name="pmid25789972">{{cite journal | vauthors = Sharma S, Javadekar SM, Pandey M, Srivastava M, Kumari R, Raghavan SC | title = Homology and enzymatic requirements of microhomology-dependent alternative end joining | journal = [[Cell Death & Disease]] | volume = 6 | issue = 3 | pages = e1697 | date = March 2015 | pmid = 25789972 | pmc = 4385936 | doi = 10.1038/cddis.2015.58 }}</ref> MMEJ is associated with frequent chromosome abnormalities such as deletions, translocations, inversions and other complex rearrangements. When PARP1 is up-regulated, MMEJ is increased, causing [[genome instability]].<ref name=Muvarak>{{cite journal | vauthors = Muvarak N, Kelley S, Robert C, Baer MR, Perrotti D, Gambacorti-Passerini C, Civin C, Scheibner K, Rassool FV | display-authors = 6 | title = c-MYC Generates Repair Errors via Increased Transcription of Alternative-NHEJ Factors, LIG3 and PARP1, in Tyrosine Kinase-Activated Leukemias | journal = [[Molecular Cancer Research]] | volume = 13 | issue = 4 | pages = 699–712 | date = April 2015 | pmid = 25828893 | pmc = 4398615 | doi = 10.1158/1541-7786.MCR-14-0422 }}</ref> PARP1 is up-regulated and MMEJ is increased in tyrosine kinase-activated leukemias.<ref name=Muvarak />
PARP1 is also over-expressed when its promoter region [[ETS1|ETS]] site is [[epigenetics|epigenetically]] hypomethylated, and this contributes to progression to endometrial cancer,<ref name="pmid23762867">{{cite journal | vauthors = Bi FF, Li D, Yang Q | title = Hypomethylation of ETS transcription factor binding sites and upregulation of PARP1 expression in endometrial cancer | journal = [[BioMed Research International]] | volume = 2013 | pages = 946268 | year = 2013 | pmid = 23762867 | pmc = 3666359 | doi = 10.1155/2013/946268 | doi-access = free }}</ref> BRCA-mutated ovarian cancer,<ref name="pmid24448423">{{cite journal | vauthors = Li D, Bi FF, Cao JM, Cao C, Li CY, Liu B, Yang Q | title = Poly (ADP-ribose) polymerase 1 transcriptional regulation: a novel crosstalk between histone modification H3K9ac and ETS1 motif hypomethylation in BRCA1-mutated ovarian cancer | journal = [[Oncotarget]] | volume = 5 | issue = 1 | pages = 291–7 | date = January 2014 | pmid = 24448423 | pmc = 3960209 | doi = 10.18632/oncotarget.1549 }}</ref> and BRCA-mutated serous ovarian cancer.<ref name="pmid23442605">{{cite journal | vauthors = Bi FF, Li D, Yang Q | title = Promoter hypomethylation, especially around the E26 transformation-specific motif, and increased expression of poly (ADP-ribose) polymerase 1 in BRCA-mutated serous ovarian cancer | journal = [[BMC Cancer]] | volume = 13 | pages = 90 | date = February 2013 | pmid = 23442605 | pmc = 3599366 | doi = 10.1186/1471-2407-13-90 | doi-access = free }}</ref>
PARP1 is also over-expressed in a number of other cancers, including neuroblastoma,<ref name="pmid25563294">{{cite journal | vauthors = Newman EA, Lu F, Bashllari D, Wang L, Opipari AW, Castle VP | title = Alternative NHEJ Pathway Components Are Therapeutic Targets in High-Risk Neuroblastoma | journal = [[Molecular Cancer Research]] | volume = 13 | issue = 3 | pages = 470–82 | date = March 2015 | pmid = 25563294 | doi = 10.1158/1541-7786.MCR-14-0337 | doi-access = free }}</ref> HPV infected oropharyngeal carcinoma,<ref name="pmid30087144">{{cite journal | vauthors = Liu Q, Ma L, Jones T, Palomero L, Pujana MA, Martinez-Ruiz H, Ha PK, Murnane J, Cuartas I, Seoane J, Baumann M, Linge A, Barcellos-Hoff MH | display-authors = 6 | title = Subjugation of TGFβ Signaling by Human Papilloma Virus in Head and Neck Squamous Cell Carcinoma Shifts DNA Repair from Homologous Recombination to Alternative End Joining | journal = [[Clinical Cancer Research]] | volume = 24 | issue = 23 | pages = 6001–6014 | date = December 2018 | pmid = 30087144 | doi = 10.1158/1078-0432.CCR-18-1346 | doi-access = free }}</ref> testicular and other germ cell tumors,<ref name="pmid23486608">{{cite journal | vauthors = Mego M, Cierna Z, Svetlovska D, Macak D, Machalekova K, Miskovska V, Chovanec M, Usakova V, Obertova J, Babal P, Mardiak J | display-authors = 6 | title = PARP expression in germ cell tumours | journal = [[Journal of Clinical Pathology]] | volume = 66 | issue = 7 | pages = 607–12 | date = July 2013 | pmid = 23486608 | doi = 10.1136/jclinpath-2012-201088 | s2cid = 535704 }}</ref>
Cancers are very often '''deficient''' in expression of one or more DNA repair genes, but '''over-expression''' of a DNA repair gene is less usual in cancer. For instance, at least 36 DNA repair enzymes, when mutationally defective in germ line cells, cause increased risk of cancer (hereditary [[cancer syndrome]]s).{{Citation needed|date=December 2019|reason=removed citation to predatory publisher content}} (Also see [[DNA repair-deficiency disorder]].) Similarly, at least 12 DNA repair genes have frequently been found to be epigenetically repressed in one or more cancers.{{Citation needed|date=December 2019|reason=removed citation to predatory publisher content}} (See also [[DNA repair#Frequencies of epimutations in DNA repair genes|Epigenetically reduced DNA repair and cancer]].) Ordinarily, deficient expression of a DNA repair enzyme results in increased un-repaired DNA damage which, through replication errors ([[DNA repair#Translesion synthesis|translesion synthesis]]), lead to mutations and cancer. However, PARP1 mediated [[microhomology-mediated end joining|MMEJ]] repair is highly inaccurate, so in this case, over-expression, rather than under-expression, apparently leads to cancer.
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===Aging===
PARP activity (which is mainly due to PARP1) measured in the permeabilized mononuclear [[leukocyte]] blood cells of thirteen mammalian species (rat, guinea pig, rabbit, marmoset, sheep, pig, cattle, pigmy chimpanzee, horse, donkey, gorilla elephant and man) correlates with maximum lifespan of the species.<ref name="pmid1465394">{{cite journal | vauthors = Grube K, Bürkle A | title = Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span | journal = [[Proceedings of the National Academy of Sciences of the United States of America]] | volume = 89 | issue = 24 | pages = 11759–63 | date = December 1992 | pmid = 1465394 | pmc = 50636 | doi = 10.1073/pnas.89.24.11759 | bibcode = 1992PNAS...8911759G | doi-access = free }}</ref> [[Lymphoblastoid]] cell lines established from blood samples of humans who were centenarians (100 years old or older) have significantly higher PARP activity than cell lines from younger (20 to 70 years old) individuals.<ref name="pmid9587069">{{cite journal | vauthors = Muiras ML, Müller M, Schächter F, Bürkle A | title = Increased poly(ADP-ribose) polymerase activity in lymphoblastoid cell lines from centenarians | journal = [[Journal of Molecular Medicine]] | volume = 76 | issue = 5 | pages = 346–54 | date = April 1998 | pmid = 9587069 | doi = 10.1007/s001090050226 | s2cid = 24616650 }}</ref> The [[Werner syndrome ATP-dependent helicase|Wrn]] protein is deficient in persons with [[Werner syndrome]], a human premature aging disorder. PARP1 and Wrn proteins are part of a complex involved in the processing of [[DNA repair|DNA breaks]].<ref name="pmid12707040">{{cite journal | vauthors = Lebel M, Lavoie J, Gaudreault I, Bronsard M, Drouin R | title = Genetic cooperation between the Werner syndrome protein and poly(ADP-ribose) polymerase-1 in preventing chromatid breaks, complex chromosomal rearrangements, and cancer in mice | journal = [[The American Journal of Pathology]] | volume = 162 | issue = 5 | pages = 1559–69 | date = May 2003 | pmid = 12707040 | pmc = 1851180 | doi = 10.1016/S0002-9440(10)64290-3 }}</ref> These findings indicate a linkage between longevity and PARP-mediated DNA repair capability. Furthermore, PARP can also act against production of reactive oxygen species, which may contribute to longevity by inhibiting oxidative damage to DNA and proteins.<ref name="pmid29511347">{{cite journal | vauthors = Liu Q, Gheorghiu L, Drumm M, Clayman R, Eidelman A, Wszolek MF, Olumi A, Feldman A, Wang M, Marcar L, Citrin DE, Wu CL, Benes CH, Efstathiou JA, Willers H | display-authors = 6 | title = PARP-1 inhibition with or without ionizing radiation confers reactive oxygen species-mediated cytotoxicity preferentially to cancer cells with mutant TP53 | journal = [[Oncogene (journal)|Oncogene]] | volume = 37 | issue = 21 | pages = 2793–2805 | date = May 2018 | pmid = 29511347 | pmc = 5970015 | doi = 10.1038/s41388-018-0130-6 }}</ref> These observations suggest that PARP activity contributes to mammalian longevity, consistent with the [[DNA damage theory of aging]].{{Citation needed|date=December 2019|reason=removed citation to predatory publisher content}}
PARP1 appears to be [[resveratrol]]'s primary functional target through its interaction with the tyrosyl tRNA synthetase (TyrRS).<ref name=Sajish>{{cite journal | vauthors = Sajish M, Schimmel P | title = A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol | journal = [[Nature (journal)|Nature]] | volume = 519 | issue = 7543 | pages = 370–3 | date = March 2015 | pmid = 25533949 | pmc = 4368482 | doi = 10.1038/nature14028 | bibcode = 2015Natur.519..370S }}</ref> Tyrosyl tRNA synthetase translocates to the nucleus under stress conditions stimulating NAD<sup>+</sup>-dependent auto-poly-[[ADP-ribosylation]] of PARP1,<ref name=Sajish /> thereby altering the functions of PARP1 from a chromatin architectural protein to a DNA damage responder and transcription regulator.<ref name="pmid25136112">{{cite journal | vauthors = Muthurajan UM, Hepler MR, Hieb AR, Clark NJ, Kramer M, Yao T, Luger K | title = Automodification switches PARP-1 function from chromatin architectural protein to histone chaperone | journal = [[Proceedings of the National Academy of Sciences of the United States of America]] | volume = 111 | issue = 35 | pages = 12752–7 | date = September 2014 | pmid = 25136112 | pmc = 4156740 | doi = 10.1073/pnas.1405005111 | bibcode = 2014PNAS..11112752M | doi-access = free }}</ref>
The messenger RNA level and protein level of PARP1 is controlled, in part, by the expression level of the [[ETS1]] transcription factor which interacts with multiple ETS1 binding sites in the promoter region of PARP1.<ref name=Soldatenkov>{{cite journal | vauthors = Soldatenkov VA, Albor A, Patel BK, Dreszer R, Dritschilo A, Notario V | title = Regulation of the human poly(ADP-ribose) polymerase promoter by the ETS transcription factor | journal = [[Oncogene (journal)|Oncogene]] | volume = 18 | issue = 27 | pages = 3954–62 | date = July 1999 | pmid = 10435618 | doi = 10.1038/sj.onc.1202778 | doi-access = free }}</ref> The degree to which the ETS1 transcription factor can bind to its binding sites on the PARP1 promoter depends on the methylation status of the [[CpG site#CpG islands in promoters|CpG islands]] in the ETS1 binding sites in the PARP1 promoter.<ref name="pmid23762867"/> If these CpG islands in ETS1 binding sites of the PARP1 promoter are [[epigenetics|epigenetically]] hypomethylated, PARP1 is expressed at an elevated level.<ref name="pmid23762867"/><ref name="pmid24448423"/>
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Cells from older humans (69 to 75 years of age) have a [[Gene expression#Regulation of gene expression|constitutive]] expression level of both PARP1 and PARP2 genes reduced by half, compared to their levels in young adult humans (19 to 26 years old). However, centenarians (humans aged 100 to 107 years of age) have constitutive expression of PARP1 at levels similar to those of young individuals.<ref name=Chevanne>{{cite journal | vauthors = Chevanne M, Calia C, Zampieri M, Cecchinelli B, Caldini R, Monti D, Bucci L, Franceschi C, Caiafa P | display-authors = 6 | 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 |url=https://www.researchgate.net/publication/6313423}}</ref> This high level of PARP1 expression in centenarians was shown to allow more efficient repair of [[Hydrogen peroxide|H<sub>2</sub>O<sub>2</sub>]] sublethal oxidative DNA damage.<ref name=Chevanne /> Higher DNA repair is thought to contribute to longevity (see [[DNA damage theory of aging]]). The high constitutive levels of PARP1 in centenarians were thought to be due to altered epigenetic control of PARP1 expression.<ref name=Chevanne />
Both [[sirtuin 1]] and PARP1 have a roughly equal affinity for the NAD+ that both enzymes require for activity.<ref name="pmid28417163">{{cite journal | vauthors = Hwang ES, Song SB | title = Nicotinamide is an inhibitor of SIRT1 in vitro, but can be a stimulator in cells | journal = [[Cellular and Molecular Life Sciences]] | volume = 74 | issue = 18 | pages =
== Role in cell death ==
Following severe DNA damage, excessive activation of PARP1 can lead to cell death.<ref>{{cite journal | vauthors = Erdélyi K, Bakondi E, Gergely P, Szabó C, Virág L | title = Pathophysiologic role of oxidative stress-induced poly(ADP-ribose) polymerase-1 activation: focus on cell death and transcriptional regulation | journal = Cellular and Molecular Life Sciences | volume = 62 | issue = 7–8 | pages = 751–759 | date = April 2005 | pmid = 15868400 | doi = 10.1007/s00018-004-4506-0 | s2cid = 43817844 }}</ref> Initially, overactivation of the enzyme was linked to apoptotic cell death<ref>{{cite journal | vauthors = Tanaka Y, Yoshihara K, Tohno Y, Kojima K, Kameoka M, Kamiya T | title = Inhibition and down-regulation of poly(ADP-ribose) polymerase results in a marked resistance of HL-60 cells to various apoptosis-inducers | journal = Cellular and Molecular Biology | volume = 41 | issue = 6 | pages = 771–781 | date = September 1995 | pmid = 8535170 | url = https://pubmed.ncbi.nlm.nih.gov/8535170/ }}</ref><ref>{{cite journal | vauthors = Rosenthal DS, Ding R, Simbulan-Rosenthal CM, Vaillancourt JP, Nicholson DW, Smulson M | title = Intact cell evidence for the early synthesis, and subsequent late apopain-mediated suppression, of poly(ADP-ribose) during apoptosis | journal = Experimental Cell Research | volume = 232 | issue = 2 | pages = 313–321 | date = May 1997 | pmid = 9168807 | doi = 10.1006/excr.1997.3536 | doi-access = free }}</ref> but later, PARP1-mediated cell death turned out to show characteristics of necrotic cell death (i.e. early plasma membrane disruption, structural and functional mitochondrial alterations).<ref>{{cite journal | vauthors = Virág L, Scott GS, Cuzzocrea S, Marmer D, Salzman AL, Szabó C | title = Peroxynitrite-induced thymocyte apoptosis: the role of caspases and poly (ADP-ribose) synthetase (PARS) activation | journal = Immunology | volume = 94 | issue = 3 | pages = 345–355 | date = July 1998 | pmid = 9767416 | doi = 10.1046/j.1365-2567.1998.00534.x | pmc = 1364252 }}</ref><ref>{{cite journal | vauthors = Virág L, Salzman AL, Szabó C | title = Poly(ADP-ribose) synthetase activation mediates mitochondrial injury during oxidant-induced cell death | journal = Journal of Immunology | volume = 161 | issue = 7 | pages = 3753–3759 | date = October 1998 | doi = 10.4049/jimmunol.161.7.3753 | pmid = 9759901 | s2cid = 5734113 | url = https://journals.aai.org/jimmunol/article/161/7/3753/7226/Poly-ADP-Ribose-Synthetase-Activation-Mediates }}</ref> These findings provided explanation for previous and subsequent reports demonstrating tissue protective effects of PARP inhibitors and the PARP1 knockout phenotypes in various models of ischemia-reperfusion injury (e.g. in stroke, in the heart and in the gut) where oxidative stress-induced cell death is a central cellular event.<ref>{{cite journal | vauthors = Virág L, Szabó C | title = The therapeutic potential of poly(ADP-ribose) polymerase inhibitors | journal = Pharmacological Reviews | volume = 54 | issue = 3 | pages = 375–429 | date = September 2002 | pmid = 12223530 | doi = 10.1124/pr.54.3.375 | s2cid = 27100634 }}</ref> Later, apoptosis inducing factor (AIF; a misnomer) was identified as a key mediator of the PARP1-mediated regulated necrotic cell death pathway termed parthanatos.<ref>{{cite journal | vauthors = Yu SW, Wang H, Poitras MF, Coombs C, Bowers WJ, Federoff HJ, Poirier GG, Dawson TM, Dawson VL | display-authors = 6 | title = Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor | journal = Science | volume = 297 | issue = 5579 | pages = 259–263 | date = July 2002 | pmid = 12114629 | doi = 10.1126/science.1072221 | bibcode = 2002Sci...297..259Y | s2cid = 22991897 | doi-access = }}</ref>
== Plant PARP1 ==
Plants have a PARP1 with substantial similarity to animal PARP1, and roles of poly(ADP-ribosyl)ation in plant responses to DNA damage, infection and other stresses have been studied.<ref>{{cite journal | vauthors = Briggs AG, Bent AF | title = Poly(ADP-ribosyl)ation in plants | journal = [[Trends in Plant Science]] | volume = 16 | issue = 7 | pages = 372–80 | date = July 2011 | pmid = 21482174 | doi = 10.1016/j.tplants.2011.03.008 }}</ref><ref>{{cite journal | vauthors = Feng B, Liu C, Shan L, He P | title = Protein ADP-Ribosylation Takes Control in Plant-Bacterium Interactions | journal = [[PLOS Pathogens]] | volume = 12 | issue = 12 | pages = e1005941 | date = December 2016 | pmid = 27907213 | pmc = 5131896 | doi = 10.1371/journal.ppat.1005941 | doi-access = free }}</ref> Intriguingly, in ''Arabidopsis thaliana'' (and presumably other plants), PARP2 plays more significant roles than PARP1 in protective responses to DNA damage and bacterial pathogenesis.<ref name=Song2015>{{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 }}</ref> The plant PARP2 carries PARP regulatory and catalytic domains with only intermediate similarity to PARP1, and carries N-terminal SAP DNA binding motifs rather than the Zn-finger DNA binding motifs of plant and animal PARP1 proteins.<ref name=Song2015 />
== Interactions ==
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{{div col|colwidth=10em}}
* [[Aprataxin|APTX]]<ref name=pmid15044383/><ref name="pmid5555565">{{cite journal | vauthors = Morgan HE, Jefferson LS, Wolpert EB, Rannels DE | title = Regulation of protein synthesis in heart muscle. II. Effect of amino acid levels and insulin on ribosomal aggregation | journal = [[The Journal of Biological Chemistry]] | volume = 246 | issue = 7 | pages = 2163–70 | date = April 1971 | doi = 10.1016/S0021-9258(19)77203-2 | pmid = 5555565 | doi-access = free }}</ref>
* [[MYBL2]]<ref name="pmid10744766">{{cite journal | vauthors = Cervellera MN, Sala A | title = Poly(ADP-ribose) polymerase is a B-MYB coactivator | journal = [[The Journal of Biological Chemistry]] | volume = 275 | issue = 14 | pages = 10692–6 | date = April 2000 | pmid = 10744766 | doi = 10.1074/jbc.275.14.10692 | doi-access = free }}</ref>
* [[RELA]]<ref name="pmid11590148">{{cite journal | vauthors = Hassa PO, Covic M, Hasan S, Imhof R, Hottiger MO | title = The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function | journal = [[The Journal of Biological Chemistry]] | volume = 276 | issue = 49 | pages = 45588–97 | date = December 2001 | pmid = 11590148 | doi = 10.1074/jbc.M106528200 | doi-access = free }}</ref>
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== Further reading ==
* {{cite journal | vauthors = Rosado MM, Bennici E, Novelli F, Pioli C | title = Beyond DNA repair, the immunological role of PARP-1 and its siblings | journal = [[Immunology (journal)|Immunology]] | volume = 139 | issue = 4 | pages = 428–37 | date = August 2013 | pmid = 23489378 | pmc = 3719060 | doi = 10.1111/imm.12099
{{PDB Gallery|geneid=142}}
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