Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis

被引:14
|
作者
Morada, Mary [1 ]
Smid, Ondrej [5 ]
Hampl, Vladimir [5 ]
Sutak, Robert [1 ,5 ]
Lam, Brian
Rappelli, Paola [3 ,4 ]
Diessi, Daniele [3 ,4 ]
Fiori, Pier L. [3 ,4 ]
Tachezy, Jan [5 ]
Yarlett, Nigel [1 ,2 ]
机构
[1] Pace Univ, Haskins Labs, New York, NY 10038 USA
[2] Pace Univ, Dept Chem & Phys Sci, New York, NY 10038 USA
[3] Univ Sassari, Dept Biomed Sci, Div Expt & Clin Microbiol, I-07100 Sassari, Italy
[4] Univ Sassari, Ctr Biotechnol Dev & Biodivers Res, I-07100 Sassari, Italy
[5] Charles Univ Prague, Dept Parasitol, Prague, Czech Republic
关键词
Trichomonas vaginalis; Hydrogenosome; Mitochondrion-like organelle; Arginine dihydrolase pathway; Arginine deiminase; DIHYDROLASE PATHWAY; MEMBRANE; SEQUENCE;
D O I
10.1016/j.molbiopara.2010.10.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 vagina lis 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. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:51 / 54
页数:4
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