Journal
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Volume 206, Issue 1-2, Pages 29-38Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2016.01.006
Keywords
Trichomonas; Hydrogenosomes; OsmC; Glycine decarboxylase complex; Peroxide; Lipoate
Categories
Funding
- Czech Science Foundation [13-09208J]
- Biotechnology and Biomedicine Center of the Academy of Sciences and Charles University from the European Regional Development Fund [CZ.1.05/1.1.00/02.0109]
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Osmotically inducible protein (OsmC) and organic hydroperoxide resistance protein (Ohr) are small, thiol-dependent peroxidases that comprise a family of prokaryotic protective proteins central to the defense against deleterious effects of organic hydroperoxides, which are reactive molecules that are formed during interactions between the host immune system and pathogens. Trichomonas vaginalis, a sexually transmitted parasite of humans, possesses OsmC homologues in its hydrogenosomes, anaerobic mitochondrial organelles that harbor enzymes and pathways that are sensitive to oxidative damage. The glycine decarboxylase complex (GDC), which consists of four proteins (i.e., L, H, P and T), is in eukaryotes exclusively mitochondrial enzymatic system that catalyzes oxidative decarboxylation and deamination of glycine. However, trichomonad hydrogenosomes contain only the L and H proteins, whose physiological functions are unknown. Here, we found that the hydrogenosomal L and H proteins constitute a lipoate-dependent redox system that delivers electrons from reduced nicotinamide adenine dinucleotide (NADH) to OsmC for the reductive detoxification of peroxides. Our searches of genome databases revealed that, in addition to prokaryotes, homologues of OsmC/Ohr family proteins with predicted mitochondrial localization are present in various eukaryotic lineages. Therefore, we propose that the novel OsmC-GDC-based redox system may not be limited to T. vaginalis. (C) 2016 Elsevier B.V. All rights reserved.
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