Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis

Mol Biochem Parasitol. 2011 Mar;176(1):51-4. doi: 10.1016/j.molbiopara.2010.10.004. Epub 2010 Nov 11.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Gene Expression Regulation, Enzymologic
  • Hydrolases / genetics
  • Hydrolases / metabolism*
  • Organelles / enzymology
  • Phylogeny
  • Protein Transport
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Trichomonas vaginalis / enzymology*
  • Trichomonas vaginalis / genetics*

Substances

  • Recombinant Fusion Proteins
  • Hydrolases
  • arginine deiminase