Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis |
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Authors: | Morada Mary Smid Ondrej Hampl Vladimir Sutak Robert Lam Brian Rappelli Paola Dessì Daniele Fiori Pier L Tachezy Jan Yarlett Nigel |
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Affiliation: | Haskins Laboratories, Pace University, New York, NY 10038, USA. |
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Abstract: | 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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