Morada, Mary and Smid, Ondrej and Hampl, Vladimir and Sutak, Robert and Lam, Brian and Rappelli, Paola and Dessì, Daniele and Fiori, Pier Luigi and Tachezy, Jan and Yarlett, Nigel (2011) Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis. Molecular and Biochemical Parasitology, Vol. 176 (1), p. 51-54. eISSN 1872-9428. Article.
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The arginine dihydrolase (ADH) pathway has an analogous function to the urea cycle in mitochondria-containing cells, by removing nitrogen from amino acids and generating ATP. Subcellular localization of the ADH pathway enzymes in Trichomonas vaginalis revealed that arginine deiminase (ADI) localizes to the hydrogenosome, a mitochondrion-like organelle of anaerobic protists. However the other enzymes of the ADH pathway, ornithine carbamyltransferase and carbamate kinase localize to the cytosol. Three gene sequences of T. vaginalis ADI (ADI 1–3) were identified in the T. vaginalis genome, all having putative mitochondrial targeting sequences. The ADI sequences were cloned and used to probe T. vaginalis using a carboxyterminal di-hemogglutinin epitope tag which demonstrated co-localization with malic enzyme confirming the hydrogenosome localization of this enzyme.
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