Characterization of an unusual thioredoxin-type protein in African trypanosomes.

LEROUX, ALEJANDRO E.; KRAUTH-SIEGEL, R. LUISE

Girona

Conferencia; Thiol-Based Redox Regulation & Signaling; 2014

Gordon Research Conference

Trypanosoma brucei possesses a unique redox metabolism which is based on the dithiol trypanothione (T(SH)2) and the thioredoxin homologue, tryparedoxin. Both, the de novo synthesis and the reduction of trypanothione are fulfilled by enzymes that are exclusively located in the cytosol. The mitochondrion of T. brucei contains a 2 Cys-peroxiredoxin as well as a non selenium glutathione peroxidase both of which in vitro use the T(SH)2/tryparedoxin couple. However, tryparedoxin is also not detectable in the organelle and the physiological electron source for the mitochondrial peroxidases is completely unknown. Our current work aims at the characterization of a thioredoxin-type protein which does not have any counterpart outside African trypanosomes, of which three different algorithms predict a mitochondrial localization. The biochemical properties of the recombinant protein the role within the parasite, evaluated by the generation of conditional knock out bloodstream forms, will be presented.