INVESTIGADORES
ARIAS Diego Gustavo
artículos
Título:
Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp.
Autor/es:
ARIAS, DIEGO G.; CABEZA, MATÍAS S.; ERBEN, ESTEBAN, D.; CARRANZA, PEDRO, G.; LUJAN, HUGO D.; TÉLLEZ IÑÓN, MARÍA T.; IGLESIAS, ALBERTO A.; GUERRERO, SERGIO A.
Revista:
FREE RADICAL BIOLOGY AND MEDICINE
Editorial:
ELSEVIER SCIENCE INC
Referencias:
Año: 2011 vol. 50 p. 37 - 46
ISSN:
0891-5849
Resumen:
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.