Počet záznamů: 1  

Characterization of Two Mitochondrial Flavin Adenine Dinucleotide-Dependent Glycerol-3-Phosphate Dehydrogenases in Trypanosoma brucei

  1. 1.
    SYSNO ASEP0421249
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevCharacterization of Two Mitochondrial Flavin Adenine Dinucleotide-Dependent Glycerol-3-Phosphate Dehydrogenases in Trypanosoma brucei
    Tvůrce(i) Škodová, Ingrid (BC-A) ORCID
    Verner, Zdeněk (BC-A)
    Bringaud, F. (FR)
    Fabian, P. (SK)
    Lukeš, Julius (BC-A) RID, ORCID
    Horváth, A. (SK)
    Zdroj.dok.Eukaryotic Cell - ISSN 1535-9778
    Roč. 12, č. 12 (2013), s. 1664-1673
    Poč.str.10 s.
    Forma vydáníTištěná - P
    Jazyk dok.eng - angličtina
    Země vyd.US - Spojené státy americké
    Klíč. slovaalternative NADH dehydrogenase ; inducible expression system ; blood-stream forms ; complex-I ; procyclic trypanosomes ; sleeping sickness ; oxidase ; localization ; metabolism ; cycle
    Vědní obor RIVEB - Genetika a molekulární biologie
    CEPGAP305/11/2179 GA ČR - Grantová agentura ČR
    GD206/09/H026 GA ČR - Grantová agentura ČR
    LH12104 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy
    Institucionální podporaBC-A - RVO:60077344
    UT WOS000327712200010
    DOI10.1128/EC.00152-13
    AnotaceGlycerol-3-phosphate dehydrogenases (G3PDHs) constitute a shuttle that serves for regeneration of NAD(+) reduced during glycolysis. This NAD-dependent enzyme is employed in glycolysis and produces glycerol-3-phosphate from dihydroxyacetone phosphate, while its flavin adenine dinucleotide (FAD)-dependent homologue catalyzes a reverse reaction coupled to the respiratory chain. Trypanosoma brucei possesses two FAD-dependent G3PDHs. While one of them (mitochondrial G3PDH [mtG3PDH]) has been attributed to the mitochondrion and seems to be directly involved in G3PDH shuttle reactions, the function of the other enzyme (putative G3PDH [putG3PDH]) remains unknown. In this work, we used RNA interference and protein overexpression and tagging to shed light on the relative contributions of both FAD-G3PDHs to overall cellular metabolism. Our results indicate that mtG3PDH is essential for the bloodstream stage of T. brucei, while in the procyclic stage the enzyme is dispensable. Expressed putG3PDH-V5 was localized to the mitochondrion, and the data obtained by digitonin permeabilization, Western blot analysis, and immunofluorescence indicate that putG3PDH is located within the mitochondrion.
    PracovištěBiologické centrum (od r. 2006)
    KontaktDana Hypšová, eje@eje.cz, Tel.: 387 775 214
    Rok sběru2014
Počet záznamů: 1  

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