Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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Externe Organisationen

  • University of Western Australia
  • University of Tokyo (UTokyo)
  • Rheinisch-Westfälische Technische Hochschule Aachen (RWTH)
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Details

OriginalspracheEnglisch
Aufsatznummer72
FachzeitschriftFrontiers in Plant Science
Jahrgang8
AusgabenummerFEBRUARY
PublikationsstatusVeröffentlicht - 8 Feb. 2017

Abstract

In eukaryotes the presence of the dimeric phospholipid cardiolipin (CL) is limited to the mitochondrial membranes. It resides predominantly in the inner membrane where it interacts with components of the mitochondrial electron transfer chain. CL deficiency has previously been shown to affect abundances of the plant NADH-dehydrogenase complex and its association with dimeric cyctochrome c reductase. Using an Arabidopsis thaliana knock-out mutant for the final enzyme of CL biosynthesis we here extend current knowledge on the dependence of plant respiration on CL. By correlating respiratory enzyme abundances with enzymatic capacities in mitochondria isolated from wild type, CL deficient and CL complemented heterotrophic cell culture lines a new picture of the participation of CL in plant respiration is emerging. Data indicate a loss of a general reduction of respiratory capacity in CL deficient mitochondria which cannot solely be attributed to decreased abundances or capacities of mitochondrial electron transfer protein complexes and supercomplexes. Instead, it most likely is the result of a loss of the mobile electron carrier cytochrome c. Furthermore, enzymes of the tricarboxylic acid cycle are found to have lower maximum activities in the mutant, including the succinate dehydrogenase complex. Interestingly, abundance of the latter is not altered, indicative of a direct impact of CL deficiency on the enzymatic capacity of this electron transfer chain protein complex.

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Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways. / Petereit, Jakob; Katayama, Kenta; Lorenz, Christin et al.
in: Frontiers in Plant Science, Jahrgang 8, Nr. FEBRUARY, 72, 08.02.2017.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Petereit, J, Katayama, K, Lorenz, C, Ewert, L, Schertl, P, Kitsche, A, Wada, H, Frentzen, M, Braun, HP & Eubel, H 2017, 'Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways', Frontiers in Plant Science, Jg. 8, Nr. FEBRUARY, 72. https://doi.org/10.3389/fpls.2017.00072
Petereit, J., Katayama, K., Lorenz, C., Ewert, L., Schertl, P., Kitsche, A., Wada, H., Frentzen, M., Braun, H. P., & Eubel, H. (2017). Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways. Frontiers in Plant Science, 8(FEBRUARY), Artikel 72. https://doi.org/10.3389/fpls.2017.00072
Petereit J, Katayama K, Lorenz C, Ewert L, Schertl P, Kitsche A et al. Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways. Frontiers in Plant Science. 2017 Feb 8;8(FEBRUARY):72. doi: 10.3389/fpls.2017.00072
Petereit, Jakob ; Katayama, Kenta ; Lorenz, Christin et al. / Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways. in: Frontiers in Plant Science. 2017 ; Jahrgang 8, Nr. FEBRUARY.
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title = "Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways",
abstract = "In eukaryotes the presence of the dimeric phospholipid cardiolipin (CL) is limited to the mitochondrial membranes. It resides predominantly in the inner membrane where it interacts with components of the mitochondrial electron transfer chain. CL deficiency has previously been shown to affect abundances of the plant NADH-dehydrogenase complex and its association with dimeric cyctochrome c reductase. Using an Arabidopsis thaliana knock-out mutant for the final enzyme of CL biosynthesis we here extend current knowledge on the dependence of plant respiration on CL. By correlating respiratory enzyme abundances with enzymatic capacities in mitochondria isolated from wild type, CL deficient and CL complemented heterotrophic cell culture lines a new picture of the participation of CL in plant respiration is emerging. Data indicate a loss of a general reduction of respiratory capacity in CL deficient mitochondria which cannot solely be attributed to decreased abundances or capacities of mitochondrial electron transfer protein complexes and supercomplexes. Instead, it most likely is the result of a loss of the mobile electron carrier cytochrome c. Furthermore, enzymes of the tricarboxylic acid cycle are found to have lower maximum activities in the mutant, including the succinate dehydrogenase complex. Interestingly, abundance of the latter is not altered, indicative of a direct impact of CL deficiency on the enzymatic capacity of this electron transfer chain protein complex.",
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T1 - Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways

AU - Petereit, Jakob

AU - Katayama, Kenta

AU - Lorenz, Christin

AU - Ewert, Linda

AU - Schertl, Peter

AU - Kitsche, Andreas

AU - Wada, Hajime

AU - Frentzen, Margrit

AU - Braun, Hans Peter

AU - Eubel, Holger

N1 - Funding information: We acknowledge financial support by Deutsche Forschungsge-meinschaft (DFG) for MF and HE (EU54/4-1).

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Y1 - 2017/2/8

N2 - In eukaryotes the presence of the dimeric phospholipid cardiolipin (CL) is limited to the mitochondrial membranes. It resides predominantly in the inner membrane where it interacts with components of the mitochondrial electron transfer chain. CL deficiency has previously been shown to affect abundances of the plant NADH-dehydrogenase complex and its association with dimeric cyctochrome c reductase. Using an Arabidopsis thaliana knock-out mutant for the final enzyme of CL biosynthesis we here extend current knowledge on the dependence of plant respiration on CL. By correlating respiratory enzyme abundances with enzymatic capacities in mitochondria isolated from wild type, CL deficient and CL complemented heterotrophic cell culture lines a new picture of the participation of CL in plant respiration is emerging. Data indicate a loss of a general reduction of respiratory capacity in CL deficient mitochondria which cannot solely be attributed to decreased abundances or capacities of mitochondrial electron transfer protein complexes and supercomplexes. Instead, it most likely is the result of a loss of the mobile electron carrier cytochrome c. Furthermore, enzymes of the tricarboxylic acid cycle are found to have lower maximum activities in the mutant, including the succinate dehydrogenase complex. Interestingly, abundance of the latter is not altered, indicative of a direct impact of CL deficiency on the enzymatic capacity of this electron transfer chain protein complex.

AB - In eukaryotes the presence of the dimeric phospholipid cardiolipin (CL) is limited to the mitochondrial membranes. It resides predominantly in the inner membrane where it interacts with components of the mitochondrial electron transfer chain. CL deficiency has previously been shown to affect abundances of the plant NADH-dehydrogenase complex and its association with dimeric cyctochrome c reductase. Using an Arabidopsis thaliana knock-out mutant for the final enzyme of CL biosynthesis we here extend current knowledge on the dependence of plant respiration on CL. By correlating respiratory enzyme abundances with enzymatic capacities in mitochondria isolated from wild type, CL deficient and CL complemented heterotrophic cell culture lines a new picture of the participation of CL in plant respiration is emerging. Data indicate a loss of a general reduction of respiratory capacity in CL deficient mitochondria which cannot solely be attributed to decreased abundances or capacities of mitochondrial electron transfer protein complexes and supercomplexes. Instead, it most likely is the result of a loss of the mobile electron carrier cytochrome c. Furthermore, enzymes of the tricarboxylic acid cycle are found to have lower maximum activities in the mutant, including the succinate dehydrogenase complex. Interestingly, abundance of the latter is not altered, indicative of a direct impact of CL deficiency on the enzymatic capacity of this electron transfer chain protein complex.

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