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PARP2

From Wikipedia, the free encyclopedia
PARP2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPARP2, ADPRT2, ADPRTL2, ADPRTL3, ARTD2, PARP-2, pADPRT-2, poly(ADP-ribose) polymerase 2
External IDsOMIM: 607725; MGI: 1341112; HomoloGene: 4004; GeneCards: PARP2; OMA:PARP2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001042618
NM_005484

NM_009632

RefSeq (protein)

NP_001036083
NP_005475

NP_033762

Location (UCSC)Chr 14: 20.34 – 20.36 MbChr 14: 51.05 – 51.06 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Poly [ADP-ribose] polymerase 2 is an enzyme that in humans is encoded by the PARP2 gene.[5][6][7] It is one of the PARP family of enzymes.

Function

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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.[7]

In the plant species Arabidopsis thaliana, PARP2 plays more significant roles than PARP1 in protective responses to DNA damage and bacterial pathogenesis.[8] The plant PARP2 carries N-terminal SAP DNA binding motifs rather than the Zn-finger DNA binding motifs of plant and animal PARP1 proteins.[8]

PARP inhibitor drugs

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

Interactions

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PARP2 has been shown to interact with XRCC1.[9]

PARP2 also interacts with HPF1.[10][11][12]

PARP2 binds to and bridges blunt DNA ends.[12][13][14]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000129484Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036023Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Johansson M (May 1999). "A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues". Genomics. 57 (3): 442–5. doi:10.1006/geno.1999.5799. PMID 10329013.
  6. ^ Yélamos J, Schreiber V, Dantzer F (April 2008). "Toward specific functions of poly(ADP-ribose) polymerase-2". Trends in Molecular Medicine. 14 (4): 169–78. doi:10.1016/j.molmed.2008.02.003. PMID 18353725.
  7. ^ a b "Entrez Gene: PARP2 poly (ADP-ribose) polymerase family, member 2".
  8. ^ a b Song J, Keppler BD, Wise RR, Bent AF (May 2015). "PARP2 Is the Predominant Poly(ADP-Ribose) Polymerase in Arabidopsis DNA Damage and Immune Responses". PLOS Genetics. 11 (5): e1005200. doi:10.1371/journal.pgen.1005200. PMC 4423837. PMID 25950582.
  9. ^ Schreiber V, Amé JC, Dollé P, Schultz I, Rinaldi B, Fraulob V, Ménissier-de Murcia J, de Murcia G (June 2002). "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1". The Journal of Biological Chemistry. 277 (25): 23028–36. doi:10.1074/jbc.M202390200. PMID 11948190.
  10. ^ Gibbs-Seymour I, Fontana P, Rack JG, Ahel I (5 May 2016). "HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity". Molecular Cell. 62 (3): 432–442. doi:10.1016/j.molcel.2016.03.008. PMC 4858568. PMID 27067600.
  11. ^ Suskiewicz MJ, Zobel F, Ogden TE, Fontana P, Ariza A, Yang JC, Zhu K, Bracken L, Hawthorne WJ, Ahel D, Neuhaus D, Ahel I (March 2020). "HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation". Nature. 579 (7800): 598–602. Bibcode:2020Natur.579..598S. doi:10.1038/s41586-020-2013-6. PMC 7104379. PMID 32028527.
  12. ^ a b Gaullier G, Roberts G, Muthurajan UM, Bowerman S, Rudolph J, Mahadevan J, Jha A, Rae PS, Luger K (3 November 2020). "Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1". PLOS ONE. 15 (11): e0240932. Bibcode:2020PLoSO..1540932G. doi:10.1371/journal.pone.0240932. PMC 7608914. PMID 33141820.
  13. ^ Obaji E, Haikarainen T, Lehtiö L (14 December 2018). "Structural basis for DNA break recognition by ARTD2/PARP2". Nucleic Acids Research. 46 (22): 12154–12165. doi:10.1093/nar/gky927. PMC 6294510. PMID 30321391.
  14. ^ Bilokapic S, Suskiewicz MJ, Ahel I, Halic M (September 2020). "Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin". Nature. 585 (7826): 609–613. Bibcode:2020Natur.585..609B. doi:10.1038/s41586-020-2725-7. PMC 7529888. PMID 32939087.

Further reading

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