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Fernández Villamil, S.H.; Baltanás, R.; Alonso, G.D.; Vilchez Larrea, S.C.; Torres, H.N.; Flawiá, M.M. "TcPARP: A DNA damage-dependent poly(ADP-ribose) polymerase from Trypanosoma cruzi" (2008) International Journal for Parasitology. 38(3-4):277-287
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Abstract:

Poly(ADP-ribose) polymerase (PARP) is a nuclear enzyme present in most eukaryotes and has been involved in processes such as DNA repair and gene expression. The poly(ADP-ribose) polymer (PAR) is mainly catabolised by poly(ADP-ribose) glycohydrolase. Here, we describe the cloning and characterisation of a PARP from Trypanosoma cruzi (TcPARP). The recombinant enzyme (Mr = 65) required DNA for catalytic activity and it was strongly enhanced by nicked DNA. Histones purified from T. cruzi increased TcPARP activity and the covalent attachment of [32P]ADP-ribose moieties to histones was demonstrated. TcPARP required no magnesium or any other metal ion cofactor for its activity. The enzyme was inhibited by 3-aminobenzamide, nicotinamide, theophylline and thymidine but not by menadione. We demonstrated an automodification reaction of TcPARP, and that the removal of attached PAR from this protein resulted in an increase of its activity. The enzyme was expressed in all parasite stages (amastigotes, epimastigotes and trypomastigotes). When T. cruzi epimastigotes were exposed to DNA-damaging agents such as hydrogen peroxide or β-lapachone, PAR drastically increased in the nucleus, thus confirming PAR synthesis in vivo and suggesting a physiological role for PARP in trypanosomatid DNA repair signalling. © 2007 Australian Society for Parasitology Inc.

Registro:

Documento: Artículo
Título:TcPARP: A DNA damage-dependent poly(ADP-ribose) polymerase from Trypanosoma cruzi
Autor:Fernández Villamil, S.H.; Baltanás, R.; Alonso, G.D.; Vilchez Larrea, S.C.; Torres, H.N.; Flawiá, M.M.
Filiación:Instituto de Investigaciones en Ingeniería Genética y Biología Molecular, Consejo Nacional de Investigaciones Científicas y Técnicas, Departamento de Fisiología, Biología Molecular y Celular, Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina
Palabras clave:DNA repair signalling; PARG; PARP; Trypanosoma cruzi; 3 aminobenzamide; beta lapachone; histone; hydrogen peroxide; menadione; nicotinamide; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase; theophylline; thymidine; clone; damage; DNA; enzyme activity; gene expression; inhibition; protozoan; recombination; article; catalysis; DNA damage; enzyme activity; gene expression; in vivo study; molecular cloning; nonhuman; nucleotide sequence; protein analysis; protein synthesis; sequence analysis; Trypanosoma cruzi; Animals; Base Sequence; Cloning, Molecular; DNA Damage; DNA Repair; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Escherichia coli; Gene Expression; Immunoblotting; Immunohistochemistry; Life Cycle Stages; Molecular Sequence Data; Parasitology; Poly Adenosine Diphosphate Ribose; Poly(ADP-ribose) Polymerases; Sequence Analysis, DNA; Trypanosoma cruzi; Eukaryota; Trypanosoma cruzi; Trypanosomatidae
Año:2008
Volumen:38
Número:3-4
Página de inicio:277
Página de fin:287
DOI: http://dx.doi.org/10.1016/j.ijpara.2007.08.003
Título revista:International Journal for Parasitology
Título revista abreviado:Int. J. Parasitol.
ISSN:00207519
CODEN:IJPYB
CAS:3 aminobenzamide, 3544-24-9; beta lapachone, 4707-32-8; histone, 9062-68-4; hydrogen peroxide, 7722-84-1; menadione, 58-27-5; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase, 58319-92-9; nicotinamide, 11032-50-1, 98-92-0; theophylline, 58-55-9, 5967-84-0, 8055-07-0, 8061-56-1, 99007-19-9; thymidine, 50-89-5; Poly Adenosine Diphosphate Ribose, 26656-46-2; Poly(ADP-ribose) Polymerases, EC 2.4.2.30
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207519_v38_n3-4_p277_FernandezVillamil

Referencias:

  • Ame, J.C., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., de Murcia, G., PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase (1999) J. Biol. Chem., 274, pp. 17860-17868
  • Ame, J.C., Spenlehauer, C., de Murcia, G., The PARP superfamily (2004) Bioessays, 26, pp. 882-893
  • Augustin, A., Spenlehauer, C., Dumond, H., Menissier-De Murcia, J., Piel, M., Schmit, A.C., Apiou, F., De Murcia, G., PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression (2003) J. Cell. Sci., 116, pp. 1551-1562
  • Banasik, M., Komura, H., Shimoyama, M., Ueda, K., Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase (1992) J. Biol. Chem., 267, pp. 1569-1575
  • Bonicalzi, M.E., Haince, J.F., Droit, A., Poirier, G.G., Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when? (2005) Cell. Mol. Life Sci., 62, pp. 739-750
  • Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
  • Brochu, G., Duchaine, C., Thibeault, L., Lagueux, J., Shah, G.M., Poirier, G.G., Mode of action of poly(ADP-ribose) glycohydrolase (1994) Biochim. Biophys. Acta, 1219, pp. 342-350
  • Buki, K.G., Bauer, P.I., Hakam, A., Kun, E., Identification of domains of poly(ADP-ribose) polymerase for protein binding and self-association (1995) J. Biol. Chem., 270, pp. 3370-3377
  • Chang, P., Jacobson, M.K., Mitchison, T.J., Poly(ADP-ribose) is required for spindle assembly and structure (2004) Nature, 432, pp. 645-649
  • da Cunha, J.P., Nakayasu, E.S., Elias, M.C., Pimenta, D.C., Tellez-Inon, M.T., Rojas, F., Munoz, M.J., Schenkman, S., Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle (2005) Mol. Biochem. Parasitol., 140, pp. 75-86
  • D'Amours, D., Desnoyers, S., D'Silva, I., Poirier, G.G., Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions (1999) Biochem. J., 342 (PART 2), pp. 249-268
  • Davidovic, L., Vodenicharov, M., Affar, E.B., Poirier, G.G., Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism (2001) Exp. Cell Res., 268, pp. 7-13
  • de Murcia, G., Menissier de Murcia, J., Poly(ADP-ribose) polymerase: a molecular nick-sensor (1994) Trends Biochem. Sci., 19, pp. 172-176
  • Diefenbach, J., Burkle, A., Introduction to poly(ADP-ribose) metabolism (2005) Cell. Mol. Life Sci., 62, pp. 721-730
  • Faraone Mennella, M.R., Castellano, S., De Luca, P., Discenza, A., Gambacorta, A., Nicolaus, B., Farina, B., Comparison of the ADP-ribosylating thermozyme from Sulfolobus solfataricus and the mesophilic poly(ADP-ribose) polymerases (2000) FEMS Microbiol. Lett., 192, pp. 9-14
  • Faraone-Mennella, M.R., Gambacorta, A., Nicolaus, B., Farina, B., Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus (1998) Biochem. J., 335 (PART 2), pp. 441-447
  • Faraone-Mennella, M.R., Chromatin architecture and functions: the role(s) of poly(ADP-RIBOSE) polymerase and poly(ADPribosyl)ation of nuclear proteins (2005) Biochem. Cell Biol., 83, pp. 396-404
  • Ferro, A.M., Olivera, B.M., Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism (1982) J Biol Chem, 257, pp. 7808-7813
  • Gagne, J.P., Hendzel, M.J., Droit, A., Poirier, G.G., The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives (2006) Curr. Opin. Cell Biol., 18, pp. 145-151
  • Goijman, S.G., Stoppani, A.O., Effects of beta-lapachone, a peroxide-generating quinone, on macromolecule synthesis and degradation in Trypanosoma cruzi (1985) Arch. Biochem. Biophys., 240, pp. 273-280
  • Hassa, P.O., Haenni, S.S., Buerki, C., Meier, N.I., Lane, W.S., Owen, H., Gersbach, M., Hottiger, M.O., Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription (2005) J. Biol. Chem., 280, pp. 40450-40464
  • Hassa, P.O., Haenni, S.S., Elser, M., Hottiger, M.O., Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? (2006) Microbiol. Mol. Biol. Rev., 70, pp. 789-829
  • Isola, E.L., Lammel, E.M., Gonzalez Cappa, S.M., Trypanosoma cruzi: differentiation to metacyclic trypomastigotes in the presence of ADP-ribosyltransferase inhibitors (1987) Exp. Parasitol., 64, pp. 424-429
  • Kim, M.Y., Mauro, S., Gevry, N., Lis, J.T., Kraus, W.L., NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1 (2004) Cell, 119, pp. 803-814
  • Kim, M.Y., Zhang, T., Kraus, W.L., Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal (2005) Genes Dev., 19, pp. 1951-1967
  • Kofler, B., Wallraff, E., Herzog, H., Schneider, R., Auer, B., Schweiger, M., Purification and characterization of NAD+:ADP-ribosyltransferase (polymerizing) from Dictyostelium discoideum (1993) Biochem. J., 293 (PART 1), pp. 275-281
  • Kraus, W.L., Lis, J.T., PARP goes transcription (2003) Cell, 113, pp. 677-683
  • Kun, E., Kirsten, E., Mendeleyev, J., Ordahl, C.P., Regulation of the enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3, and ATP (2004) Biochemistry, 43, pp. 210-216
  • Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
  • Lepiniec, L., Babiychuk, E., Kushnir, S., Van Montagu, M., Inze, D., Characterization of an Arabidopsis thaliana cDNA homologue to animal poly(ADP-ribose) polymerase (1995) FEBS Lett., 364, pp. 103-108
  • Lonskaya, I., Potaman, V.N., Shlyakhtenko, L.S., Oussatcheva, E.A., Lyubchenko, Y.L., Soldatenkov, V.A., Regulation of poly(ADP-ribose) polymerase-1 by DNA structure-specific binding (2005) J. Biol. Chem., 280, pp. 17076-17083
  • Malanga, M., Althaus, F.R., The role of poly(ADP-ribose) in the DNA damage signaling network (2005) Biochem. Cell. Biol., 83, pp. 354-364
  • Mendoza-Alvarez, H., Alvarez-Gonzalez, R., Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular (1993) J. Biol. Chem., 268, pp. 22575-22580
  • Novy, R., Drott, D., Yaeger, K., Mierenhof, R., Overcoming the codon bias of E. coli for enhanced protein expression (2001) inNovations, 12, pp. 1-3
  • Oliver, A.W., Ame, J.C., Roe, S.M., Good, V., de Murcia, G., Pearl, L.H., Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2 (2004) Nucleic Acids Res., 32, pp. 456-464
  • Oliver, F.J., Menissier-de Murcia, J., de Murcia, G., Poly(ADP-ribose) polymerase in the cellular response to DNA damage, apoptosis, and disease (1999) Am. J. Hum. Genet., 64, pp. 1282-1288
  • Otto, H., Reche, P.A., Bazan, F., Dittmar, K., Haag, F., Koch-Nolte, F., In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs) (2005) BMC Genomics, 6, p. 139
  • Pereira, C.A., Alonso, G.D., Paveto, M.C., Iribarren, A., Cabanas, M.L., Torres, H.N., Flawia, M.M., Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites (2000) J. Biol. Chem., 275, pp. 1495-1501
  • Petermann, E., Keil, C., Oei, S.L., Importance of poly(ADP-ribose) polymerases in the regulation of DNA-dependent processes (2005) Cell. Mol. Life Sci., 62, pp. 731-738
  • Petzold, S.J., Booth, B.A., Leimbach, G.A., Berger, N.A., Purification and properties of poly(ADP-ribose) polymerase from lamb thymus (1981) Biochemistry, 20, pp. 7075-7081
  • Podesta, D., Garcia-Herreros, M.I., Cannata, J.J., Stoppani, A.O., Fernandez Villamil, S.H., Purification and properties of poly(ADP-ribose)polymerase from Crithidia fasciculata. Automodification and poly(ADP-ribosyl)ation of DNA topoisomerase I (2004) Mol. Biochem. Parasitol., 135, pp. 211-219
  • Poirot, O., Suhre, K., Abergel, C., O'Toole, E., Notredame, C., 3DCoffee@igs: a web server for combining sequences and structures into a multiple sequence alignment (2004) Nucleic Acids Res., 32, pp. W37-W40
  • Potaman, V.N., Shlyakhtenko, L.S., Oussatcheva, E.A., Lyubchenko, Y.L., Soldatenkov, V.A., Specific binding of poly(ADP-ribose) polymerase-1 to cruciform hairpins (2005) J. Mol. Biol., 348, pp. 609-615
  • Rankin, P.W., Jacobson, E.L., Benjamin, R.C., Moss, J., Jacobson, M.K., Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo (1989) J. Biol. Chem., 264, pp. 4312-4317
  • Schreiber, V., Dantzer, F., Ame, J.C., de Murcia, G., Poly(ADP-ribose): novel functions for an old molecule (2006) Nat. Rev. Mol. Cell Biol., 7, pp. 517-528
  • Shah, G.M., Poirier, D., Duchaine, C., Brochu, G., Desnoyers, S., Lagueux, J., Verreault, A., Poirier, G.G., Methods for biochemical study of poly(ADP-ribose) metabolism in vitro and in vivo (1995) Anal. Biochem., 227, pp. 1-13
  • Tulin, A., Stewart, D., Spradling, A.C., The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development (2002) Genes Dev., 16, pp. 2108-2119
  • Ueda, K., Hayaishi, O., ADP-ribosylation (1985) Annu. Rev. Biochem., 54, pp. 73-100
  • Ushiro, H., Yokoyama, Y., Shizuta, Y., Purification and characterization of poly (ADP-ribose) synthetase from human placenta (1987) J. Biol. Chem., 262, pp. 2352-2357
  • Villamil, S.F., Podesta, D., Molina Portela, M.D., Stoppani, A., Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: enzyme inhibition by beta-lapachone (2001) Mol. Biochem. Parasitol., 115, pp. 249-256
  • Williams, G.T., Trypanosoma cruzi: inhibition of intracellular and extracellular differentiation by ADP-ribosyl transferase antagonists (1983) Exp. Parasitol., 56, pp. 409-415
  • Yoshihara, K., Hashida, T., Tanaka, Y., Ohgushi, H., Yoshihara, H., Kamiya, T., Bovine thymus poly(adenosine diphosphate ribose) polymerase (1978) J. Biol. Chem., 253, pp. 6459-6466
  • Zahradka, P., Ebisuzaki, K., Poly(ADP-ribose) polymerase is a zinc metalloenzyme (1984) Eur. J. Biochem., 142, pp. 503-509
  • Ziegler, M., Oei, S.L., A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription (2001) Bioessays, 23, pp. 543-548

Citas:

---------- APA ----------
Fernández Villamil, S.H., Baltanás, R., Alonso, G.D., Vilchez Larrea, S.C., Torres, H.N. & Flawiá, M.M. (2008) . TcPARP: A DNA damage-dependent poly(ADP-ribose) polymerase from Trypanosoma cruzi. International Journal for Parasitology, 38(3-4), 277-287.
http://dx.doi.org/10.1016/j.ijpara.2007.08.003
---------- CHICAGO ----------
Fernández Villamil, S.H., Baltanás, R., Alonso, G.D., Vilchez Larrea, S.C., Torres, H.N., Flawiá, M.M. "TcPARP: A DNA damage-dependent poly(ADP-ribose) polymerase from Trypanosoma cruzi" . International Journal for Parasitology 38, no. 3-4 (2008) : 277-287.
http://dx.doi.org/10.1016/j.ijpara.2007.08.003
---------- MLA ----------
Fernández Villamil, S.H., Baltanás, R., Alonso, G.D., Vilchez Larrea, S.C., Torres, H.N., Flawiá, M.M. "TcPARP: A DNA damage-dependent poly(ADP-ribose) polymerase from Trypanosoma cruzi" . International Journal for Parasitology, vol. 38, no. 3-4, 2008, pp. 277-287.
http://dx.doi.org/10.1016/j.ijpara.2007.08.003
---------- VANCOUVER ----------
Fernández Villamil, S.H., Baltanás, R., Alonso, G.D., Vilchez Larrea, S.C., Torres, H.N., Flawiá, M.M. TcPARP: A DNA damage-dependent poly(ADP-ribose) polymerase from Trypanosoma cruzi. Int. J. Parasitol. 2008;38(3-4):277-287.
http://dx.doi.org/10.1016/j.ijpara.2007.08.003