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Abstract:

Poly(ADP-ribose)polymerase has been purified more than 160,000-fold from Crithidia fasciculata. This is the first PARP isolated to apparent homogeneity from trypanosomatids. The purified enzyme absolutely required DNA for catalytic activity and histones enhanced it 2.5-fold, when the DNA:histone ratio was 1:1.3. The enzyme required no magnesium or any other metal ion cofactor. The apparent molecular mass of 111kDa, determined by gel filtration would correspond to a dimer of two identical 55-kDa subunits. Activity was inhibited by nicotinamide, 3-aminobenzamide, theophylline, thymidine, xanthine and hypoxanthine but not by adenosine. The enzyme was localized to the cell nucleus. Our findings suggest that covalent poly(ADP-ribosyl)ation of PARP itself or DNA topoisomerase I resulted in the inhibition of their activities and provide an initial biochemical characterization of this covalent post-translational modification in trypanosomatids. © 2004 Elsevier B.V. All rights reserved.

Registro:

Documento: Artículo
Título:Purification and properties of poly(ADP-ribose)polymerase from Crithidia fasciculata: Automodification and poly(ADP-ribosyl)ation of DNA topoisomerase I
Autor:Podestá, D.; García-Herreros, M.I.; Cannata, J.J.B.; Stoppani, A.O.M.; Fernández Villamil, S.H.
Filiación:Bioenergetics Research Centre, School of Medicine, University of Buenos Aires, Paraguay 2155, 1121 Buenos Aires, Argentina
Inst. Invest. Ing. Genet. Y Biol. M., Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina
Palabras clave:Crithidia fasciculata; D,L-dithiothreitol; DNA topoisomerase I; DTT; NAD+; PARP; Poly(ADP-ribose)polymerase; TCA; Topo; Trichloroacetic acid; β-Me; β-mercaptoethanol; β-nicotinamide adenine dinucleotide; adenosine; DNA topoisomerase; hypoxanthine; nicotinamide; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase; theophylline; thymidine; xanthine; article; catalysis; cell nucleus; controlled study; Crithidia fasciculata; enzyme activity; enzyme inhibition; enzyme isolation; enzyme purification; gel filtration; molecular dynamics; nonhuman; priority journal; Crithidia fasciculata
Año:2004
Volumen:135
Número:2
Página de inicio:211
Página de fin:219
DOI: http://dx.doi.org/10.1016/j.molbiopara.2004.02.005
Título revista:Molecular and Biochemical Parasitology
Título revista abreviado:Mol. Biochem. Parasitol.
ISSN:01666851
CODEN:MBIPD
CAS:adenosine, 58-61-7; DNA topoisomerase, 80449-01-0; hypoxanthine, 68-94-0; nicotinamide, 11032-50-1, 98-92-0; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase, 58319-92-9; theophylline, 58-55-9, 5967-84-0, 8055-07-0, 8061-56-1, 99007-19-9; thymidine, 50-89-5; xanthine, 69-89-6
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v135_n2_p211_Podesta

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Citas:

---------- APA ----------
Podestá, D., García-Herreros, M.I., Cannata, J.J.B., Stoppani, A.O.M. & Fernández Villamil, S.H. (2004) . Purification and properties of poly(ADP-ribose)polymerase from Crithidia fasciculata: Automodification and poly(ADP-ribosyl)ation of DNA topoisomerase I. Molecular and Biochemical Parasitology, 135(2), 211-219.
http://dx.doi.org/10.1016/j.molbiopara.2004.02.005
---------- CHICAGO ----------
Podestá, D., García-Herreros, M.I., Cannata, J.J.B., Stoppani, A.O.M., Fernández Villamil, S.H. "Purification and properties of poly(ADP-ribose)polymerase from Crithidia fasciculata: Automodification and poly(ADP-ribosyl)ation of DNA topoisomerase I" . Molecular and Biochemical Parasitology 135, no. 2 (2004) : 211-219.
http://dx.doi.org/10.1016/j.molbiopara.2004.02.005
---------- MLA ----------
Podestá, D., García-Herreros, M.I., Cannata, J.J.B., Stoppani, A.O.M., Fernández Villamil, S.H. "Purification and properties of poly(ADP-ribose)polymerase from Crithidia fasciculata: Automodification and poly(ADP-ribosyl)ation of DNA topoisomerase I" . Molecular and Biochemical Parasitology, vol. 135, no. 2, 2004, pp. 211-219.
http://dx.doi.org/10.1016/j.molbiopara.2004.02.005
---------- VANCOUVER ----------
Podestá, D., García-Herreros, M.I., Cannata, J.J.B., Stoppani, A.O.M., Fernández 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. 2004;135(2):211-219.
http://dx.doi.org/10.1016/j.molbiopara.2004.02.005