Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites

This work contains the first description of a guanidino kinase in a flagellar unicellular parasite. The enzyme phosphorylates L-arginine and was characterized in preparations from Trypanosoma cruzi, the ethiological agent of Chagas' disease. The activity requires ATP and a divalent cation. Unde...

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Autores principales:	Pereira, C.A., Alonso, G.D., Paveto, M.C., Iribarren, A., Cabanas, M.L., Torres, H.N., Flawiá, M.M.
Formato:	JOUR
Materias:	adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Arthropoda Mammalia Protozoa Trypanosoma
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00219258_v275_n2_p1495_Pereira
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00219258_v275_n2_p1495_Pereira
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spelling	todo:paper_00219258_v275_n2_p1495_Pereira2023-10-03T14:22:58Z 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. Flawiá, M.M. adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi This work contains the first description of a guanidino kinase in a flagellar unicellular parasite. The enzyme phosphorylates L-arginine and was characterized in preparations from Trypanosoma cruzi, the ethiological agent of Chagas' disease. The activity requires ATP and a divalent cation. Under Standard assay conditions (1 mM L-arginine), the presence of 5-fold higher concentrations of canavanine or histidine produced a greater than 50% enzyme inhibition. The base sequence of this enzyme revealed an open reading frame of 357 amino acids and a molecular weight of 40,201. The amino acid sequence shows all of the characteristic consensus blocks of the ATP:guanidino phosphotransferase family and a putative 'actinin-type' actin-binding domain. The highest amino acid identities of the T. cruzi sequence, about 70%, were with arginine kinases from Arthropoda. Southern and chromosome blots revealed that the kinase is encoded by a single-copy gene. Moreover, Northern blot analysis showed an mRNA subpopulation of about 2.0 kilobases, and Western blotting of T. cruzi-soluble polypeptides revealed a 40-kDa band. The finding in the parasite of a phosphagen and its biosynthetic pathway, which are totally different from those in mammalian host tissues, points out this arginine kinase as a possible chemotherapy target for Chagas' disease. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219258_v275_n2_p1495_Pereira
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi
spellingShingle	adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi Pereira, C.A. Alonso, G.D. Paveto, M.C. Iribarren, A. Cabanas, M.L. Torres, H.N. Flawiá, M.M. Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
topic_facet	adenosine triphosphate arginine arginine kinase canavanine divalent cation guanidine derivative histidine messenger RNA phosphotransferase amino acid sequence article Chagas disease drug targeting energy transfer enzyme activity enzyme analysis enzyme inhibition molecular cloning molecular weight nonhuman nucleotide sequence open reading frame priority journal protozoon Trypanosoma cruzi Amino Acid Sequence Amino Acids Animals Arginine Kinase Base Sequence Cations, Divalent Chromatography, Affinity Chromosome Mapping Cloning, Molecular Genomic Library Humans Kinetics Molecular Sequence Data Phylogeny Recombinant Proteins Sequence Alignment Sequence Homology, Amino Acid Trypanosoma cruzi Arthropoda Mammalia Protozoa Trypanosoma Trypanosoma cruzi
description	This work contains the first description of a guanidino kinase in a flagellar unicellular parasite. The enzyme phosphorylates L-arginine and was characterized in preparations from Trypanosoma cruzi, the ethiological agent of Chagas' disease. The activity requires ATP and a divalent cation. Under Standard assay conditions (1 mM L-arginine), the presence of 5-fold higher concentrations of canavanine or histidine produced a greater than 50% enzyme inhibition. The base sequence of this enzyme revealed an open reading frame of 357 amino acids and a molecular weight of 40,201. The amino acid sequence shows all of the characteristic consensus blocks of the ATP:guanidino phosphotransferase family and a putative 'actinin-type' actin-binding domain. The highest amino acid identities of the T. cruzi sequence, about 70%, were with arginine kinases from Arthropoda. Southern and chromosome blots revealed that the kinase is encoded by a single-copy gene. Moreover, Northern blot analysis showed an mRNA subpopulation of about 2.0 kilobases, and Western blotting of T. cruzi-soluble polypeptides revealed a 40-kDa band. The finding in the parasite of a phosphagen and its biosynthetic pathway, which are totally different from those in mammalian host tissues, points out this arginine kinase as a possible chemotherapy target for Chagas' disease.
format	JOUR
author	Pereira, C.A. Alonso, G.D. Paveto, M.C. Iribarren, A. Cabanas, M.L. Torres, H.N. Flawiá, M.M.
author_facet	Pereira, C.A. Alonso, G.D. Paveto, M.C. Iribarren, A. Cabanas, M.L. Torres, H.N. Flawiá, M.M.
author_sort	Pereira, C.A.
title	Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
title_short	Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
title_full	Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
title_fullStr	Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
title_full_unstemmed	Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites
title_sort	trypanosoma cruzi arginine kinase characterization and cloning. a novel energetic pathway in protozoan parasites
url	http://hdl.handle.net/20.500.12110/paper_00219258_v275_n2_p1495_Pereira
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Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites

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