阴道毛滴虫中精氨酸脱亚氨酶的氢化酶体定位
Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis.
作者信息
Morada Mary, Smid Ondrej, Hampl Vladimir, Sutak Robert, Lam Brian, Rappelli Paola, Dessì Daniele, Fiori Pier L, Tachezy Jan, Yarlett Nigel
机构信息
Haskins Laboratories, Pace University, New York, NY 10038, USA.
出版信息
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.
摘要
精氨酸二水解酶（ADH）途径在含线粒体的细胞中具有与尿素循环类似的功能，即从氨基酸中去除氮并生成ATP。阴道毛滴虫中ADH途径酶的亚细胞定位显示，精氨酸脱亚氨酶（ADI）定位于氢化酶体，这是一种厌氧原生生物的线粒体样细胞器。然而，ADH途径的其他酶，鸟氨酸氨基甲酰转移酶和氨基甲酸激酶定位于细胞质。在阴道毛滴虫基因组中鉴定出了阴道毛滴虫ADI的三个基因序列（ADI 1-3），它们都具有假定的线粒体靶向序列。克隆了ADI序列，并使用羧基末端双血凝素表位标签对阴道毛滴虫进行探测，结果表明其与苹果酸酶共定位，证实了该酶在氢化酶体中的定位。
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