Lecler 2012 Curr Genet: Difference between revisions
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|journal=Curr Genet | |journal=Curr Genet | ||
|abstract=Type-II NAD(P)H dehydrogenases form a multigene family that comprise six members in the green microalga ''Chlamydomonas''. To date, only one enzyme (Nda2) located in the chloroplast has been characterized in this alga and demonstrated to participate in the reduction of the plastoquinone pool. We present here the functional characterization of Nda1. The enzyme is located on the inner face of the inner mitochondrial membrane. Its downregulation leads to a slight decrease of NADH:ferricyanide activity and of dark whole cell respiration. To determine whether the reduction of Nda1 combined with the lack of Complex I would affect mitochondrial processes, double mutants affected in both Nda1 and Complex I were isolated. Respiration and growth rates in heterotrophic conditions were significantly altered in the double mutants investigated, suggesting that Nda1 plays a role in the oxidation of matrix NADH in the absence of Complex I. | |abstract=Type-II NAD(P)H dehydrogenases form a multigene family that comprise six members in the green microalga ''Chlamydomonas''. To date, only one enzyme (Nda2) located in the chloroplast has been characterized in this alga and demonstrated to participate in the reduction of the plastoquinone pool. We present here the functional characterization of Nda1. The enzyme is located on the inner face of the inner mitochondrial membrane. Its downregulation leads to a slight decrease of NADH:ferricyanide activity and of dark whole cell respiration. To determine whether the reduction of Nda1 combined with the lack of Complex I would affect mitochondrial processes, double mutants affected in both Nda1 and Complex I were isolated. Respiration and growth rates in heterotrophic conditions were significantly altered in the double mutants investigated, suggesting that Nda1 plays a role in the oxidation of matrix NADH in the absence of Complex I. | ||
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{{Labeling | {{Labeling | ||
|area=Respiration | |area=Respiration | ||
|additional= | |organism=Algae | ||
|additional=Dark respiration | |||
}} | }} |
Latest revision as of 15:29, 8 August 2023
Lecler R, Vigeolas H, Emonds-Alt B, Cardol P, Remacle C (2012) Characterization of an internal type-II NADH dehydrogenase from Chlamydomonas reinhardtii mitochondria. Curr Genet 58:205โ16. |
Lecler R, Vigeolas H, Emonds-Alt B, Cardol P, Remacle C (2012) Curr Genet
Abstract: Type-II NAD(P)H dehydrogenases form a multigene family that comprise six members in the green microalga Chlamydomonas. To date, only one enzyme (Nda2) located in the chloroplast has been characterized in this alga and demonstrated to participate in the reduction of the plastoquinone pool. We present here the functional characterization of Nda1. The enzyme is located on the inner face of the inner mitochondrial membrane. Its downregulation leads to a slight decrease of NADH:ferricyanide activity and of dark whole cell respiration. To determine whether the reduction of Nda1 combined with the lack of Complex I would affect mitochondrial processes, double mutants affected in both Nda1 and Complex I were isolated. Respiration and growth rates in heterotrophic conditions were significantly altered in the double mutants investigated, suggesting that Nda1 plays a role in the oxidation of matrix NADH in the absence of Complex I.
Labels: MiParea: Respiration
Organism: Algae
Dark respiration