메뉴 건너뛰기




Volumn 38, Issue 3-4, 2008, Pages 277-287

TcPARP: A DNA damage-dependent poly(ADP-ribose) polymerase from Trypanosoma cruzi

Author keywords

DNA repair signalling; PARG; PARP; Trypanosoma cruzi

Indexed keywords

3 AMINOBENZAMIDE; BETA LAPACHONE; HISTONE; HYDROGEN PEROXIDE; MENADIONE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; THEOPHYLLINE; THYMIDINE;

EID: 38949160014     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpara.2007.08.003     Document Type: Article
Times cited : (28)

References (54)
  • 4
    • 0026601666 scopus 로고
    • Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase
    • Banasik M., Komura H., Shimoyama M., and Ueda K. Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase. J. Biol. Chem. 267 (1992) 1569-1575
    • (1992) J. Biol. Chem. , vol.267 , pp. 1569-1575
    • Banasik, M.1    Komura, H.2    Shimoyama, M.3    Ueda, K.4
  • 5
    • 18544384491 scopus 로고    scopus 로고
    • Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when?
    • Bonicalzi M.E., Haince J.F., Droit A., and Poirier G.G. Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when?. Cell. Mol. Life Sci. 62 (2005) 739-750
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 739-750
    • Bonicalzi, M.E.1    Haince, J.F.2    Droit, A.3    Poirier, G.G.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0028868288 scopus 로고
    • Identification of domains of poly(ADP-ribose) polymerase for protein binding and self-association
    • Buki K.G., Bauer P.I., Hakam A., and Kun E. Identification of domains of poly(ADP-ribose) polymerase for protein binding and self-association. J. Biol. Chem. 270 (1995) 3370-3377
    • (1995) J. Biol. Chem. , vol.270 , pp. 3370-3377
    • Buki, K.G.1    Bauer, P.I.2    Hakam, A.3    Kun, E.4
  • 9
    • 10344234720 scopus 로고    scopus 로고
    • Poly(ADP-ribose) is required for spindle assembly and structure
    • Chang P., Jacobson M.K., and Mitchison T.J. Poly(ADP-ribose) is required for spindle assembly and structure. Nature 432 (2004) 645-649
    • (2004) Nature , vol.432 , pp. 645-649
    • Chang, P.1    Jacobson, M.K.2    Mitchison, T.J.3
  • 11
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., and Poirier G.G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342 Pt 2 (1999) 249-268
    • (1999) Biochem. J. , vol.342 , Issue.PART 2 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 12
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • Davidovic L., Vodenicharov M., Affar E.B., and Poirier G.G. Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism. Exp. Cell Res. 268 (2001) 7-13
    • (2001) Exp. Cell Res. , vol.268 , pp. 7-13
    • Davidovic, L.1    Vodenicharov, M.2    Affar, E.B.3    Poirier, G.G.4
  • 13
    • 0000102949 scopus 로고
    • Poly(ADP-ribose) polymerase: a molecular nick-sensor
    • de Murcia G., and Menissier de Murcia J. Poly(ADP-ribose) polymerase: a molecular nick-sensor. Trends Biochem. Sci. 19 (1994) 172-176
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 172-176
    • de Murcia, G.1    Menissier de Murcia, J.2
  • 14
    • 18544381071 scopus 로고    scopus 로고
    • Introduction to poly(ADP-ribose) metabolism
    • Diefenbach J., and Burkle A. Introduction to poly(ADP-ribose) metabolism. Cell. Mol. Life Sci. 62 (2005) 721-730
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 721-730
    • Diefenbach, J.1    Burkle, A.2
  • 16
    • 0032532020 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus
    • Faraone-Mennella M.R., Gambacorta A., Nicolaus B., and Farina B. Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus. Biochem. J. 335 Pt 2 (1998) 441-447
    • (1998) Biochem. J. , vol.335 , Issue.PART 2 , pp. 441-447
    • Faraone-Mennella, M.R.1    Gambacorta, A.2    Nicolaus, B.3    Farina, B.4
  • 17
    • 24744439538 scopus 로고    scopus 로고
    • Chromatin architecture and functions: the role(s) of poly(ADP-RIBOSE) polymerase and poly(ADPribosyl)ation of nuclear proteins
    • Faraone-Mennella M.R. Chromatin architecture and functions: the role(s) of poly(ADP-RIBOSE) polymerase and poly(ADPribosyl)ation of nuclear proteins. Biochem. Cell Biol. 83 (2005) 396-404
    • (2005) Biochem. Cell Biol. , vol.83 , pp. 396-404
    • Faraone-Mennella, M.R.1
  • 18
    • 0020479276 scopus 로고
    • Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism
    • Ferro A.M., and Olivera B.M. Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism. J Biol Chem 257 (1982) 7808-7813
    • (1982) J Biol Chem , vol.257 , pp. 7808-7813
    • Ferro, A.M.1    Olivera, B.M.2
  • 19
    • 33644850114 scopus 로고    scopus 로고
    • The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives
    • Gagne J.P., Hendzel M.J., Droit A., and Poirier G.G. The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives. Curr. Opin. Cell Biol. 18 (2006) 145-151
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 145-151
    • Gagne, J.P.1    Hendzel, M.J.2    Droit, A.3    Poirier, G.G.4
  • 20
    • 0021835907 scopus 로고
    • Effects of beta-lapachone, a peroxide-generating quinone, on macromolecule synthesis and degradation in Trypanosoma cruzi
    • Goijman S.G., and Stoppani A.O. Effects of beta-lapachone, a peroxide-generating quinone, on macromolecule synthesis and degradation in Trypanosoma cruzi. Arch. Biochem. Biophys. 240 (1985) 273-280
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 273-280
    • Goijman, S.G.1    Stoppani, A.O.2
  • 21
    • 28844493947 scopus 로고    scopus 로고
    • Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription
    • Hassa P.O., Haenni S.S., Buerki C., Meier N.I., Lane W.S., Owen H., Gersbach M., Imhof R., and Hottiger M.O. Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription. J. Biol. Chem. 280 (2005) 40450-40464
    • (2005) J. Biol. Chem. , vol.280 , pp. 40450-40464
    • Hassa, P.O.1    Haenni, S.S.2    Buerki, C.3    Meier, N.I.4    Lane, W.S.5    Owen, H.6    Gersbach, M.7    Imhof, R.8    Hottiger, M.O.9
  • 22
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
    • Hassa P.O., Haenni S.S., Elser M., and Hottiger M.O. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?. Microbiol. Mol. Biol. Rev. 70 (2006) 789-829
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 23
    • 0023472424 scopus 로고
    • Trypanosoma cruzi: differentiation to metacyclic trypomastigotes in the presence of ADP-ribosyltransferase inhibitors
    • Isola E.L., Lammel E.M., and Gonzalez Cappa S.M. Trypanosoma cruzi: differentiation to metacyclic trypomastigotes in the presence of ADP-ribosyltransferase inhibitors. Exp. Parasitol. 64 (1987) 424-429
    • (1987) Exp. Parasitol. , vol.64 , pp. 424-429
    • Isola, E.L.1    Lammel, E.M.2    Gonzalez Cappa, S.M.3
  • 24
    • 10944227347 scopus 로고    scopus 로고
    • NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • Kim M.Y., Mauro S., Gevry N., Lis J.T., and Kraus W.L. NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell 119 (2004) 803-814
    • (2004) Cell , vol.119 , pp. 803-814
    • Kim, M.Y.1    Mauro, S.2    Gevry, N.3    Lis, J.T.4    Kraus, W.L.5
  • 25
    • 24344454692 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal
    • Kim M.Y., Zhang T., and Kraus W.L. Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 19 (2005) 1951-1967
    • (2005) Genes Dev. , vol.19 , pp. 1951-1967
    • Kim, M.Y.1    Zhang, T.2    Kraus, W.L.3
  • 26
    • 0027306786 scopus 로고
    • Purification and characterization of NAD+:ADP-ribosyltransferase (polymerizing) from Dictyostelium discoideum
    • Kofler B., Wallraff E., Herzog H., Schneider R., Auer B., and Schweiger M. Purification and characterization of NAD+:ADP-ribosyltransferase (polymerizing) from Dictyostelium discoideum. Biochem. J. 293 Pt 1 (1993) 275-281
    • (1993) Biochem. J. , vol.293 , Issue.PART 1 , pp. 275-281
    • Kofler, B.1    Wallraff, E.2    Herzog, H.3    Schneider, R.4    Auer, B.5    Schweiger, M.6
  • 27
    • 0038682011 scopus 로고    scopus 로고
    • PARP goes transcription
    • Kraus W.L., and Lis J.T. PARP goes transcription. Cell 113 (2003) 677-683
    • (2003) Cell , vol.113 , pp. 677-683
    • Kraus, W.L.1    Lis, J.T.2
  • 28
    • 0345824718 scopus 로고    scopus 로고
    • Regulation of the enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3, and ATP
    • Kun E., Kirsten E., Mendeleyev J., and Ordahl C.P. Regulation of the enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3, and ATP. Biochemistry 43 (2004) 210-216
    • (2004) Biochemistry , vol.43 , pp. 210-216
    • Kun, E.1    Kirsten, E.2    Mendeleyev, J.3    Ordahl, C.P.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0028906148 scopus 로고
    • Characterization of an Arabidopsis thaliana cDNA homologue to animal poly(ADP-ribose) polymerase
    • Lepiniec L., Babiychuk E., Kushnir S., Van Montagu M., and Inze D. Characterization of an Arabidopsis thaliana cDNA homologue to animal poly(ADP-ribose) polymerase. FEBS Lett. 364 (1995) 103-108
    • (1995) FEBS Lett. , vol.364 , pp. 103-108
    • Lepiniec, L.1    Babiychuk, E.2    Kushnir, S.3    Van Montagu, M.4    Inze, D.5
  • 32
    • 24744447821 scopus 로고    scopus 로고
    • The role of poly(ADP-ribose) in the DNA damage signaling network
    • Malanga M., and Althaus F.R. The role of poly(ADP-ribose) in the DNA damage signaling network. Biochem. Cell. Biol. 83 (2005) 354-364
    • (2005) Biochem. Cell. Biol. , vol.83 , pp. 354-364
    • Malanga, M.1    Althaus, F.R.2
  • 33
    • 0027441894 scopus 로고
    • Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular
    • Mendoza-Alvarez H., and Alvarez-Gonzalez R. Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular. J. Biol. Chem. 268 (1993) 22575-22580
    • (1993) J. Biol. Chem. , vol.268 , pp. 22575-22580
    • Mendoza-Alvarez, H.1    Alvarez-Gonzalez, R.2
  • 34
    • 0141442962 scopus 로고    scopus 로고
    • Overcoming the codon bias of E. coli for enhanced protein expression
    • Novy R., Drott D., Yaeger K., and Mierenhof R. Overcoming the codon bias of E. coli for enhanced protein expression. inNovations 12 (2001) 1-3
    • (2001) inNovations , vol.12 , pp. 1-3
    • Novy, R.1    Drott, D.2    Yaeger, K.3    Mierenhof, R.4
  • 35
    • 1342286058 scopus 로고    scopus 로고
    • Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2
    • Oliver A.W., Ame J.C., Roe S.M., Good V., de Murcia G., and Pearl L.H. Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. Nucleic Acids Res. 32 (2004) 456-464
    • (2004) Nucleic Acids Res. , vol.32 , pp. 456-464
    • Oliver, A.W.1    Ame, J.C.2    Roe, S.M.3    Good, V.4    de Murcia, G.5    Pearl, L.H.6
  • 36
    • 0033362084 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase in the cellular response to DNA damage, apoptosis, and disease
    • Oliver F.J., Menissier-de Murcia J., and de Murcia G. Poly(ADP-ribose) polymerase in the cellular response to DNA damage, apoptosis, and disease. Am. J. Hum. Genet. 64 (1999) 1282-1288
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 1282-1288
    • Oliver, F.J.1    Menissier-de Murcia, J.2    de Murcia, G.3
  • 37
    • 27644577665 scopus 로고    scopus 로고
    • In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
    • Otto H., Reche P.A., Bazan F., Dittmar K., Haag F., and Koch-Nolte F. In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs). BMC Genomics 6 (2005) 139
    • (2005) BMC Genomics , vol.6 , pp. 139
    • Otto, H.1    Reche, P.A.2    Bazan, F.3    Dittmar, K.4    Haag, F.5    Koch-Nolte, F.6
  • 38
    • 0033984243 scopus 로고    scopus 로고
    • Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
    • Pereira C.A., Alonso G.D., Paveto M.C., Iribarren A., Cabanas M.L., Torres H.N., and Flawia M.M. Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites. J. Biol. Chem. 275 (2000) 1495-1501
    • (2000) J. Biol. Chem. , vol.275 , pp. 1495-1501
    • Pereira, C.A.1    Alonso, G.D.2    Paveto, M.C.3    Iribarren, A.4    Cabanas, M.L.5    Torres, H.N.6    Flawia, M.M.7
  • 39
    • 18544361870 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) polymerases in the regulation of DNA-dependent processes
    • Petermann E., Keil C., and Oei S.L. Importance of poly(ADP-ribose) polymerases in the regulation of DNA-dependent processes. Cell. Mol. Life Sci. 62 (2005) 731-738
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 731-738
    • Petermann, E.1    Keil, C.2    Oei, S.L.3
  • 40
    • 0019875792 scopus 로고
    • Purification and properties of poly(ADP-ribose) polymerase from lamb thymus
    • Petzold S.J., Booth B.A., Leimbach G.A., and Berger N.A. Purification and properties of poly(ADP-ribose) polymerase from lamb thymus. Biochemistry 20 (1981) 7075-7081
    • (1981) Biochemistry , vol.20 , pp. 7075-7081
    • Petzold, S.J.1    Booth, B.A.2    Leimbach, G.A.3    Berger, N.A.4
  • 41
    • 85058721485 scopus 로고    scopus 로고
    • Purification and properties of poly(ADP-ribose)polymerase from Crithidia fasciculata. Automodification and poly(ADP-ribosyl)ation of DNA topoisomerase I
    • Podesta D., Garcia-Herreros M.I., Cannata J.J., Stoppani A.O., and 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. Mol. Biochem. Parasitol. 135 (2004) 211-219
    • (2004) Mol. Biochem. Parasitol. , vol.135 , pp. 211-219
    • Podesta, D.1    Garcia-Herreros, M.I.2    Cannata, J.J.3    Stoppani, A.O.4    Fernandez Villamil, S.H.5
  • 42
    • 3242878412 scopus 로고    scopus 로고
    • 3DCoffee@igs: a web server for combining sequences and structures into a multiple sequence alignment
    • Poirot O., Suhre K., Abergel C., O'Toole E., and Notredame C. 3DCoffee@igs: a web server for combining sequences and structures into a multiple sequence alignment. Nucleic Acids Res. 32 (2004) W37-W40
    • (2004) Nucleic Acids Res. , vol.32
    • Poirot, O.1    Suhre, K.2    Abergel, C.3    O'Toole, E.4    Notredame, C.5
  • 44
    • 0024554229 scopus 로고
    • Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo
    • Rankin P.W., Jacobson E.L., Benjamin R.C., Moss J., and Jacobson M.K. Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo. J. Biol. Chem. 264 (1989) 4312-4317
    • (1989) J. Biol. Chem. , vol.264 , pp. 4312-4317
    • Rankin, P.W.1    Jacobson, E.L.2    Benjamin, R.C.3    Moss, J.4    Jacobson, M.K.5
  • 47
    • 0037102454 scopus 로고    scopus 로고
    • The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development
    • Tulin A., Stewart D., and Spradling A.C. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 16 (2002) 2108-2119
    • (2002) Genes Dev. , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 49
    • 0023219691 scopus 로고
    • Purification and characterization of poly (ADP-ribose) synthetase from human placenta
    • Ushiro H., Yokoyama Y., and Shizuta Y. Purification and characterization of poly (ADP-ribose) synthetase from human placenta. J. Biol. Chem. 262 (1987) 2352-2357
    • (1987) J. Biol. Chem. , vol.262 , pp. 2352-2357
    • Ushiro, H.1    Yokoyama, Y.2    Shizuta, Y.3
  • 50
    • 0035400271 scopus 로고    scopus 로고
    • Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: enzyme inhibition by beta-lapachone
    • Villamil S.F., Podesta D., Molina Portela M.D., and Stoppani A. Characterization of poly(ADP-ribose)polymerase from Crithidia fasciculata: enzyme inhibition by beta-lapachone. Mol. Biochem. Parasitol. 115 (2001) 249-256
    • (2001) Mol. Biochem. Parasitol. , vol.115 , pp. 249-256
    • Villamil, S.F.1    Podesta, D.2    Molina Portela, M.D.3    Stoppani, A.4
  • 51
    • 0021018845 scopus 로고
    • Trypanosoma cruzi: inhibition of intracellular and extracellular differentiation by ADP-ribosyl transferase antagonists
    • Williams G.T. Trypanosoma cruzi: inhibition of intracellular and extracellular differentiation by ADP-ribosyl transferase antagonists. Exp. Parasitol. 56 (1983) 409-415
    • (1983) Exp. Parasitol. , vol.56 , pp. 409-415
    • Williams, G.T.1
  • 53
    • 0021475340 scopus 로고
    • Poly(ADP-ribose) polymerase is a zinc metalloenzyme
    • Zahradka P., and Ebisuzaki K. Poly(ADP-ribose) polymerase is a zinc metalloenzyme. Eur. J. Biochem. 142 (1984) 503-509
    • (1984) Eur. J. Biochem. , vol.142 , pp. 503-509
    • Zahradka, P.1    Ebisuzaki, K.2
  • 54
    • 0034985121 scopus 로고    scopus 로고
    • A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription
    • Ziegler M., and Oei S.L. A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription. Bioessays 23 (2001) 543-548
    • (2001) Bioessays , vol.23 , pp. 543-548
    • Ziegler, M.1    Oei, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.