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Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways

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 abundan...

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Autores principales: Petereit, Jakob, Katayama, Kenta, Lorenz, Christin, Ewert, Linda, Schertl, Peter, Kitsche, Andreas, Wada, Hajime, Frentzen, Margrit, Braun, Hans-Peter, Eubel, Holger
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5296312/
https://www.ncbi.nlm.nih.gov/pubmed/28228763
http://dx.doi.org/10.3389/fpls.2017.00072
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author Petereit, Jakob
Katayama, Kenta
Lorenz, Christin
Ewert, Linda
Schertl, Peter
Kitsche, Andreas
Wada, Hajime
Frentzen, Margrit
Braun, Hans-Peter
Eubel, Holger
author_facet Petereit, Jakob
Katayama, Kenta
Lorenz, Christin
Ewert, Linda
Schertl, Peter
Kitsche, Andreas
Wada, Hajime
Frentzen, Margrit
Braun, Hans-Peter
Eubel, Holger
author_sort Petereit, Jakob
collection PubMed
description 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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spelling pubmed-52963122017-02-22 Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways Petereit, Jakob Katayama, Kenta Lorenz, Christin Ewert, Linda Schertl, Peter Kitsche, Andreas Wada, Hajime Frentzen, Margrit Braun, Hans-Peter Eubel, Holger Front Plant Sci Plant Science 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. Frontiers Media S.A. 2017-02-08 /pmc/articles/PMC5296312/ /pubmed/28228763 http://dx.doi.org/10.3389/fpls.2017.00072 Text en Copyright © 2017 Petereit, Katayama, Lorenz, Ewert, Schertl, Kitsche, Wada, Frentzen, Braun and Eubel. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Petereit, Jakob
Katayama, Kenta
Lorenz, Christin
Ewert, Linda
Schertl, Peter
Kitsche, Andreas
Wada, Hajime
Frentzen, Margrit
Braun, Hans-Peter
Eubel, Holger
Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways
title Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways
title_full Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways
title_fullStr Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways
title_full_unstemmed Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways
title_short Cardiolipin Supports Respiratory Enzymes in Plants in Different Ways
title_sort cardiolipin supports respiratory enzymes in plants in different ways
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5296312/
https://www.ncbi.nlm.nih.gov/pubmed/28228763
http://dx.doi.org/10.3389/fpls.2017.00072
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