Abstract
Poly(ADP-ribosyl)ation is an immediate DNA damage-dependent posttranslational modification of histones and other nuclear proteins that contributes to the survival of injured proliferating cells. Poly(ADP-ribose) polymerases (PARPs) now constitute a large family of 18 proteins, encoded by different genes and displaying a conserved catalytic domain in which PARP-1 (113 kDa), the founding member, and PARP-2 (62 kDa) are so far the sole enzymes whose catalytic activity is immediately stimulated by DNA strand-breaks. This review summarizes our present knowledge of the structure and function of PARP-2, the closest relative to PARP-1.
Access provided by Autonomous University of Puebla. Download to read the full chapter text
Chapter PDF
Similar content being viewed by others
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
de Murcia G, Shall S, eds. From DNA Damage and Stress Signalling to Cell Death: Poly (ADP-Ribosylation) Reactions. Oxford, New York: Oxford University Press, 2000:238.
Shieh WM, Ame JC, Wilson MV et al. Poly(ADP-ribose) polymerase null mouse cells synthesize ADP-ribose polymers. J Biol Chem 1998; 273(46):30069–72.
Ame JC, Rolli V, Schreiber V et al. PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase. J Biol Chem 1999; 274(25):17860–8.
Lepiniec L, Babiychuk E, Kushnir S et al. Characterization of an Arbidopsis thaliana cDNA homologue to animal poly(ADP-ribose) polymerase. FEBS Lett 1995; 364(2):103–8.
Smith S, Giriat I, Schmitt A et al. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 1998; 282(5393):1484–7.
Kickhoefer VA, Siva AC, Kedersha NL et al. The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase. J Cell Biol 1999; 146(5):917–28.
Dantzer F, Giraud-Panis MJ, Jaco I et al. Functional Interaction between Poly(ADP-Ribose) Polymerase 2 (PARP-2) and TRF2: PARP Activity Negatively Regulates TRF2. Mol Cell Biol 2004; 24(4):1595–1607.
Aravind L, Koonin EV. SAP-a putative DNA-binding motif involved in chromosomal organization. Trends Biochem Sci 2000; 25(3):112–4.
Menissier de Murcia J, Ricoul M, Tartier L et al. Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse. EMBO J 2003; 22(9):2255–63.
Schreiber V, Ame JC, Dolle P et al. Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J Biol Chem 2002; 277(25):23028–36.
Benchoua A, Couriaud C, Guegan C et al. Active caspase-8 translocates into the nucleus of apoptotic cells to inactivate poly(ADP-ribose) polymerase-2. J Biol Chem 2002; 277(37):34217–22.
Ame JC, Schreiber V, Fraulob V et al. A bidirectional promoter connects the poly(ADP-ribose) polymerase 2 (PARP-2) gene to the gene for RNase P RNA. structure and expression of the mouse PARP-2 gene. J Biol Chem 2001; 276(14):11092–9.
Doucet-Chabeaud G, Godon C, Brutesco C et al. Ionising radiation induces the expression of PARP-1 and PARP-2 genes in Arabidopsis. Mol Genet Genomics 2001; 265(6):954–63.
Oliver AW, Ame JC, Roe SM et al. Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. Nucleic Acids Res 2004; 32(2):456–464.
Desnoyers S, Kaufmann SH, Poirier GG. Alteration of the nucleolar localization of poly(ADP-ribose) polymerase upon treatment with transcription inhibitors. Exp Cell Res 1996; 227(1):146–53.
Choo KH. Domain organization at the centromere and neocentromere. Dev Cell 2001; 1(2):165–77.
Adams RR, Carmena M, Earnshaw WC. Chromosomal passengers and the (aurora) ABCs of mitosis. Trends Cell Biol 2001; 11(2):49–54.
Earle E, Saxena A, MacDonald A et al. Poly(ADP-ribose) polymerase at active centromeres and neocentromeres at metaphase. Hum Mol Genet 2000; 9(2):187–94.
Saxena A, Wong LH, Kalitsis P et al. Poly(ADP-ribose) polymerase 2 localizes to mammalian active centromeres and interacts with PARP-1, Cenpa, Cenpb and Bub3, but not Cenpc. Hum Mol Genet 2002; 11(19):2319–29.
Saxena A, Saffery R, Wong LH et al. Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated. J Biol Chem 2002; 277(30):26921–6.
Chalmers AJ. Poly(ADP-ribose) polymerase-1 and ionizing radiation: sensor, signaller and therapeutic target. Clin Oncol (R Coll Radiol) 2004; 16(1):29–39.
Chalmers A, Johnston P, Woodcock M et al. PARP-1, PARP-2, and the cellular response to low doses of ionizing radiation. Int J Radiat Oncol Biol Phys 2004; 58(2):410–9.
Augustin A, Spenlehauer C, Dumond H et al. PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. J Cell Sci 2003; 116(Pt 8):1551–62.
Sbodio JI, Lodish HF, Chi NW. Tankyrase-2 oliomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase). Biochem J 2002; 361(Pt 3):451–9.
de Lange T. Protection of mammalian telomeres. Oncogene 2002; 21(4):532–40.
Ferreira MG, Miller KM, Cooper JP. Indecent exposure: when telomeres become uncapped. Mol Cell 2004; 13(1):7–18.
Kaminker PG, Kim SH, Taylor RD et al. TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression. J Biol Chem. 2001; 276(38):35891–9.
Griffith JD, Comeau L, Rosenfield S et al. Mammalian telomeres end in a large duplex loop. Cell 1999; 97(4):503–14.
van Steensel B, Smogorzewska A, de Lange T. TRF2 protects human teloneres from end-to-end fusions. Cell 1998; 92(3):401–13.
Masson M, Niedergang C, Schreiber V et al. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol Cell Biol 1998; 18(6):3563–71.
Okano S, Lan L, Caldecott KW et al. Spatial and temporal cellular responses to single-strand breaks in human cells. Mol Cell Biol 2003; 23(11):3974–81.
Rogakou EP, Boon C, Redon C et al. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J Cell Biol 1999; 146(5):905–16.
Tebbs RS, Flannery ML, Meneses JJ et al. Requirement for the Xrcc1 DNA base excision repair gene during early mouse development. Dev Biol 1999; 208(2):513–29.
Ludwig DL, MacInnes MA, Takiguchi Y et al. A murine AP-endonuclease gene-targeted deficiency with post-implantation embryonic progression and ionizing radiation sensitivity. Mutat Res 1998; 409(1):17–29
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2006 Landes Bioscience and Springer Science+Business Media
About this chapter
Cite this chapter
Schreiber, V. et al. (2006). PARP-2: Structure-Function Relationship. In: Poly(ADP-Ribosyl)ation. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-36005-0_2
Download citation
DOI: https://doi.org/10.1007/0-387-36005-0_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-387-33371-7
Online ISBN: 978-0-387-36005-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)