Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp.
Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focuse...
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paper:paper_08915849_v50_n1_p37_Arias2023-06-08T15:47:12Z Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp. Erben, Esteban Daniel Free radicals Methionine sulfoxide Oxidative stress Trypanosoma Trypanothione Tryparedoxin methionine sulfoxide reductase A reducing agent tryparedoxin I unclassified drug article electrophoresis Escherichia coli gene expression gene identification gene overexpression molecular cloning oxidation reduction reaction priority journal Trypanosoma brucei Trypanosoma cruzi Amino Acid Sequence Animals Cells, Cultured Cercopithecus aethiops Cloning, Molecular Metabolic Detoxication, Phase I Metabolic Networks and Pathways Methionine Sulfoxide Reductases Models, Molecular Molecular Sequence Data Oxidation-Reduction Oxidative Stress Sequence Homology Trypanosoma Trypanosoma brucei brucei Trypanosoma cruzi Vero Cells Escherichia coli Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focused on the involvement of trypanothione, a specific redox component in these organisms. However, no information is available concerning their mechanisms for repairing oxidized proteins, which would be relevant for the survival of these pathogens in the various stages of their life cycle. We report the molecular cloning of three genes encoding a putative A-type MSR in trypanosomatids. The genes were expressed in Escherichia coli, and the corresponding recombinant proteins were purified and functionally characterized. The enzymes were specific for L-Met(S)SO reduction, using Trypanosoma cruzi tryparedoxin I as the reducing substrate. Each enzyme migrated in electrophoresis with a particular profile reflecting the differences they exhibit in superficial charge. The in vivo presence of the enzymes was evidenced by immunological detection in replicative stages of T. cruzi and Trypanosoma brucei. The results support the occurrence of a metabolic pathway in Trypanosoma spp. involved in the critical function of repairing oxidized macromolecules. © 2010 Elsevier Inc. All rights reserved. Fil:Erben, E.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08915849_v50_n1_p37_Arias http://hdl.handle.net/20.500.12110/paper_08915849_v50_n1_p37_Arias |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Free radicals Methionine sulfoxide Oxidative stress Trypanosoma Trypanothione Tryparedoxin methionine sulfoxide reductase A reducing agent tryparedoxin I unclassified drug article electrophoresis Escherichia coli gene expression gene identification gene overexpression molecular cloning oxidation reduction reaction priority journal Trypanosoma brucei Trypanosoma cruzi Amino Acid Sequence Animals Cells, Cultured Cercopithecus aethiops Cloning, Molecular Metabolic Detoxication, Phase I Metabolic Networks and Pathways Methionine Sulfoxide Reductases Models, Molecular Molecular Sequence Data Oxidation-Reduction Oxidative Stress Sequence Homology Trypanosoma Trypanosoma brucei brucei Trypanosoma cruzi Vero Cells Escherichia coli Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae |
spellingShingle |
Free radicals Methionine sulfoxide Oxidative stress Trypanosoma Trypanothione Tryparedoxin methionine sulfoxide reductase A reducing agent tryparedoxin I unclassified drug article electrophoresis Escherichia coli gene expression gene identification gene overexpression molecular cloning oxidation reduction reaction priority journal Trypanosoma brucei Trypanosoma cruzi Amino Acid Sequence Animals Cells, Cultured Cercopithecus aethiops Cloning, Molecular Metabolic Detoxication, Phase I Metabolic Networks and Pathways Methionine Sulfoxide Reductases Models, Molecular Molecular Sequence Data Oxidation-Reduction Oxidative Stress Sequence Homology Trypanosoma Trypanosoma brucei brucei Trypanosoma cruzi Vero Cells Escherichia coli Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae Erben, Esteban Daniel Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp. |
topic_facet |
Free radicals Methionine sulfoxide Oxidative stress Trypanosoma Trypanothione Tryparedoxin methionine sulfoxide reductase A reducing agent tryparedoxin I unclassified drug article electrophoresis Escherichia coli gene expression gene identification gene overexpression molecular cloning oxidation reduction reaction priority journal Trypanosoma brucei Trypanosoma cruzi Amino Acid Sequence Animals Cells, Cultured Cercopithecus aethiops Cloning, Molecular Metabolic Detoxication, Phase I Metabolic Networks and Pathways Methionine Sulfoxide Reductases Models, Molecular Molecular Sequence Data Oxidation-Reduction Oxidative Stress Sequence Homology Trypanosoma Trypanosoma brucei brucei Trypanosoma cruzi Vero Cells Escherichia coli Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae |
description |
Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focused on the involvement of trypanothione, a specific redox component in these organisms. However, no information is available concerning their mechanisms for repairing oxidized proteins, which would be relevant for the survival of these pathogens in the various stages of their life cycle. We report the molecular cloning of three genes encoding a putative A-type MSR in trypanosomatids. The genes were expressed in Escherichia coli, and the corresponding recombinant proteins were purified and functionally characterized. The enzymes were specific for L-Met(S)SO reduction, using Trypanosoma cruzi tryparedoxin I as the reducing substrate. Each enzyme migrated in electrophoresis with a particular profile reflecting the differences they exhibit in superficial charge. The in vivo presence of the enzymes was evidenced by immunological detection in replicative stages of T. cruzi and Trypanosoma brucei. The results support the occurrence of a metabolic pathway in Trypanosoma spp. involved in the critical function of repairing oxidized macromolecules. © 2010 Elsevier Inc. All rights reserved. |
author |
Erben, Esteban Daniel |
author_facet |
Erben, Esteban Daniel |
author_sort |
Erben, Esteban Daniel |
title |
Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp. |
title_short |
Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp. |
title_full |
Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp. |
title_fullStr |
Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp. |
title_full_unstemmed |
Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp. |
title_sort |
functional characterization of methionine sulfoxide reductase a from trypanosoma spp. |
publishDate |
2011 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08915849_v50_n1_p37_Arias http://hdl.handle.net/20.500.12110/paper_08915849_v50_n1_p37_Arias |
work_keys_str_mv |
AT erbenestebandaniel functionalcharacterizationofmethioninesulfoxidereductaseafromtrypanosomaspp |
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1768541617455628288 |