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Difference between revisions of "Lecler 2012 Curr Genet"

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{{Publication
{{Publication
|title=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: 205–216.
|title=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 58:205–16.
|info=[https://pubmed.ncbi.nlm.nih.gov/22814755/ PMID:22814755]
|info=[https://pubmed.ncbi.nlm.nih.gov/22814755/ PMID:22814755]
|authors=Lecler R, Vigeolas H, Emonds-Alt B, Cardol P, Remacle C
|authors=Lecler R, Vigeolas H, Emonds-Alt B, Cardol P, Remacle C
|year=2012
|year=2012
|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.
|editor=[[Huete-Ortega Maria]]
|editor=[[Huete-Ortega Maria]]
}}
}}
== Cited by ==
{{Template:Cited by Huete-Ortega M 2021 MitoFit Dark respiration}}
{{Template:Cited by Huete-Ortega M 2021 MitoFit Photosynthesis protocols}}
{{Labeling
{{Labeling
|area=Respiration
|area=Respiration
|additional=Algae, Dark respiration, MitoFit 2021 Dark respiration, MitoFit 2021 Photosynthesis
|additional=Algae, Dark respiration, MitoFit 2021 Dark respiration, MitoFit 2021 Photosynthesis
}}
}}
== Cited by ==
{{Template:Cited by Huete-Ortega M 2021 MitoFit Dark respiration}}
{{Template:Cited by Huete-Ortega M 2021 MitoFit Photosynthesis protocols}}

Revision as of 11:45, 29 April 2021

Publications in the MiPMap
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 58:205–16.

Β» PMID:22814755

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.

β€’ Bioblast editor: Huete-Ortega Maria

Cited by

  • Huete-Ortega et al (2021) Substrate-uncoupler-inhibitor-titration protocols for dark respiration in Chlamydomonas reinhardtii. MitoFit Preprints 2021 (in prep).
  • Huete-Ortega et al (2021) Substrate-uncoupler-inhibitor-titration protocols for photosynthesis in Chlamydomonas reinhardtii. MitoFit Preprints 2021 (in prep).


Labels: MiParea: Respiration 






Algae, Dark respiration, MitoFit 2021 Dark respiration, MitoFit 2021 Photosynthesis