Cloning, Expression and Characterization of a Dithiol Glutaredoxin from Trypanosoma cruzi

V.E. MÁRQUEZ; D.G. ARIAS; C.V. PIATTONI; C. ROBELLO; A.A. IGLESIAS; S.A. GUERRERO

ANTIOXIDANTS & REDOX SIGNALING

MARY ANN LIEBERT INC

Lugar: New Rochelle; Año: 2010 vol. 12 p. 787 - 792

1523-0864

Glutaredoxins play an important role in cellular functionality. A putative dithiol glutaredoxin is encoded in the genome of Trypanosoma cruzi. We cloned the gene and obtained the recombinant protein, which behaved as a typical thioltransferase. Activity was variable and dependent on the nature of reducer or oxidant agent used, or both. Epimastigote extracts exhibited similar activity, suggesting the occurrence of the protein in the parasite. Results support a redox scenario in T. cruzi, with glutaredoxin being involved mainly in reduction of glutathione disulfide as well as in deglutathionylation of target proteins.