Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F11%3A10099222" target="_blank" >RIV/00216208:11310/11:10099222 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.molbiopara.2010.10.004" target="_blank" >http://dx.doi.org/10.1016/j.molbiopara.2010.10.004</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.molbiopara.2010.10.004" target="_blank" >10.1016/j.molbiopara.2010.10.004</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/LC07032" target="_blank" >LC07032: Centrum funkční genetiky</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular and Biochemical Parasitology

ISSN

0166-6851

e-ISSN

—

Svazek periodika

176

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

4

Strana od-do

51-54

Kód UT WoS článku

000287284800007

EID výsledku v databázi Scopus

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