Complex I (NADH:ubiquinone oxidoreductase) is active in but non-essential for procyclic Trypanosoma brucei
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
21074578
DOI
10.1016/j.molbiopara.2010.11.003
PII: S0166-6851(10)00280-X
Knihovny.cz E-zdroje
- MeSH
- buněčné dýchání MeSH
- genový knockdown MeSH
- malá interferující RNA genetika metabolismus MeSH
- mikrobiální viabilita * MeSH
- podjednotky proteinů genetika metabolismus MeSH
- reaktivní formy kyslíku metabolismus MeSH
- respirační komplex I genetika metabolismus MeSH
- Trypanosoma brucei brucei enzymologie růst a vývoj metabolismus fyziologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- malá interferující RNA MeSH
- podjednotky proteinů MeSH
- reaktivní formy kyslíku MeSH
- respirační komplex I MeSH
The requirement of complex I (NADH:ubiquionone oxidoreductase) for respiration in Trypanosoma brucei is controversial. Recent identification of homologues of its subunits in mitochondrial proteome resolved a question of its presence or absence. However, with one exception, no data have been available concerning the function(s) of complex I or its subunits. Here we present a functional RNAi study of three (NUBM, NUKM, NUEM) putative subunits of this complex. Although no changes were detected in growth, mitochondrial membrane potential or reactive oxygen species production in cell lines depleted for target transcript, the NUBM and NUKM RNAi knock-downs showed decreased specific NADH:ubiquinone oxidoreductase activity. Moreover, glycerol gradients of all cell lines revealed the presence of two distinct peaks of NADH dehydrogenase activity, with shifted sensitivity to inhibitors of complex I upon RNAi induction. Thus complex I is not only present in the procyclic stage of T. brucei 29-13 strain, but it does participate in electron transport chain.
Citace poskytuje Crossref.org
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