Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis

Three gene sequences of T. vaginalis ADI having mitochondrial targeting sequences were identified in the T. vaginalis genome. Molecular and biochemical data obtained using the cloned ADI demonstrated hydrogenosomal localization of this enzyme. [Display omitted] ▶ Arginine deiminase (ADI) localizes t...

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Published in:Molecular and biochemical parasitology 2011-03, Vol.176 (1), p.51-54
Main Authors: Morada, Mary, Smid, Ondrej, Hampl, Vladimir, Sutak, Robert, Lam, Brian, Rappelli, Paola, Dessì, Daniele, Fiori, Pier L., Tachezy, Jan, Yarlett, Nigel
Format: Article
Language:English
Subjects:
ADH
ADI
Arginine deiminase
arginine dihydrolase
Arginine dihydrolase pathway
Gene Expression Regulation, Enzymologic
Hydrogenosome
Hydrolases - genetics
Hydrolases - metabolism
Mitochondrion-like organelle
OCT
Organelles - enzymology
ornithine carbamyltransferase
Phylogeny
Protein Transport
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Trichomonas vaginalis
Trichomonas vaginalis - enzymology
Trichomonas vaginalis - genetics
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Summary:Three gene sequences of T. vaginalis ADI having mitochondrial targeting sequences were identified in the T. vaginalis genome. Molecular and biochemical data obtained using the cloned ADI demonstrated hydrogenosomal localization of this enzyme. [Display omitted] ▶ Arginine deiminase (ADI) localizes to T. vaginalis hydrogenosomes. ▶ Three ADI sequences were identified in the T. vaginalis genome. ▶ All ADI genes had mitochondrial targetting sequences. ▶ Proteinase k treated ADI-1 transfected hydrogenosomes was visible by immunoblot. ▶ Proteinase k treatment of lysed ADI-1 transfected hydrogenosmes had no immunoblot signal. 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.
ISSN:0166-6851
1872-9428
DOI:10.1016/j.molbiopara.2010.10.004