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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2017
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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. |
format | Online Article Text |
id | pubmed-5296312 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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