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  Identification of the 2-Hydroxyglutarate and Isovaleryl-CoA Dehydrogenases as Alternative Electron Donors Linking Lysine Catabolism to the Electron Transport Chain of Arabidopsis Mitochondria

Araujo, W. L., Ishizaki, K., Nunes-Nesi, A., Larson, T. R., Tohge, T., Krahnert, I., et al. (2010). Identification of the 2-Hydroxyglutarate and Isovaleryl-CoA Dehydrogenases as Alternative Electron Donors Linking Lysine Catabolism to the Electron Transport Chain of Arabidopsis Mitochondria. The Plant Cell, 22(5), 1549-1563. doi:10.1105/tpc.110.075630.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2479-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8413-6
Genre: Journal Article

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 Creators:
Araujo, W. L.1, Author              
Ishizaki, K.2, Author
Nunes-Nesi, A.1, Author              
Larson, T. R.2, Author
Tohge, T.1, Author              
Krahnert, I.1, Author              
Witt, S.1, Author              
Obata, T.1, Author              
Schauer, N.1, Author              
Graham, I. A.2, Author
Leaver, C. J.2, Author
Fernie, A. R.1, Author              
Affiliations:
1Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753339              
2External Organizations, ou_persistent22              

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Free keywords: flavoprotein-ubiquinone oxidoreductase leaf senescence beta-oxidation chlorophyll breakdown gas-chromatography extended darkness pipecolic acid amino-acids plants metabolism
 Abstract: The process of dark-induced senescence in plants is relatively poorly understood, but a functional electron-transfer flavoprotein/electron-transfer flavoprotein: ubiquinone oxidoreductase (ETF/ETFQO) complex, which supports respiration during carbon starvation, has recently been identified. Here, we studied the responses of Arabidopsis thaliana mutants deficient in the expression of isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase to extended darkness and other environmental stresses. Evaluations of the mutant phenotypes following carbon starvation induced by extended darkness identify similarities to those exhibited by mutants of the ETF/ETFQO complex. Metabolic profiling and isotope tracer experimentation revealed that isovaleryl-CoA dehydrogenase is involved in degradation of the branched-chain amino acids, phytol, and Lys, while 2-hydroxyglutarate dehydrogenase is involved exclusively in Lys degradation. These results suggest that isovaleryl-CoA dehydrogenase is the more critical for alternative respiration and that a series of enzymes, including 2-hydroxyglutarate dehydrogenase, plays a role in Lys degradation. Both physiological and metabolic phenotypes of the isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase mutants were not as severe as those observed for mutants of the ETF/ETFQO complex, indicating some functional redundancy of the enzymes within the process. Our results aid in the elucidation of the pathway of plant Lys catabolism and demonstrate that both isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase act as electron donors to the ubiquinol pool via an ETF/ETFQO-mediated route.

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Language(s): eng - English
 Dates: 2010-05-272010
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: ISI:000279253200012
DOI: 10.1105/tpc.110.075630
ISSN: 1532-298X (Electronic)1040-4651 (Linking)
URI: ://000279253200012http://www.plantcell.org/content/22/5/1549.full.pdf
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Title: The Plant Cell
  Abbreviation : Plant C
Source Genre: Journal
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Publ. Info: Rockville : American Society of Plant Physiologists
Pages: - Volume / Issue: 22 (5) Sequence Number: - Start / End Page: 1549 - 1563 Identifier: Other: 1532-298X
CoNE: https://pure.mpg.de/cone/journals/resource/1532-298X