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  Analysis of a Range of Catabolic Mutants Provides Evidence That Phytanoyl-Coenzyme A Does Not Act as a Substrate of the Electron-Transfer Flavoprotein/Electron-Transfer Flavoprotein:Ubiquinone Oxidoreductase Complex in Arabidopsis during Dark-Induced Senescence

Araujo, W. L., Ishizaki, K., Nunes-Nesi, A., Tohge, T., Larson, T. R., Krahnert, I., et al. (2011). Analysis of a Range of Catabolic Mutants Provides Evidence That Phytanoyl-Coenzyme A Does Not Act as a Substrate of the Electron-Transfer Flavoprotein/Electron-Transfer Flavoprotein:Ubiquinone Oxidoreductase Complex in Arabidopsis during Dark-Induced Senescence. Plant Physiology, 157(1), 55-69. doi:10.​1104/​pp.​111.​182188.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-228C-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-83C6-9
Genre: Journal Article

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Araujo, W. L.1, Author              
Ishizaki, K.2, Author
Nunes-Nesi, A.1, Author              
Tohge, T.1, Author              
Larson, T. R.2, Author
Krahnert, I.1, Author              
Balbo, I.1, Author              
Witt, S.1, Author              
Doermann, P.3, 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, escidoc:1753339              
2External Organizations, escidoc:persistent22              
3Plant Lipids, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, escidoc:1753347              

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Free keywords: acid alpha-oxidation acyl-coa dehydrogenases beta-oxidation chlorophyll breakdown mass-spectrometry refsums-disease ubiquinone oxidoreductase gas-chromatography extended darkness leaf senescence
 Abstract: The process of dark-induced senescence in plants is not fully understood, however, the functional involvement of an electron-transfer flavoprotein/electron-transfer flavoprotein: ubiquinone oxidoreductase (ETF/ETFQO), has been demonstrated. Recent studies have revealed that the enzymes isovaleryl-coenzyme A (CoA) dehydrogenase and 2-hydroxyglutarate dehydrogenase act as important electron donors to this complex. In addition both enzymes play a role in the breakdown of cellular carbon storage reserves with isovaleryl-CoA dehydrogenase being involved in degradation of the branched-chain amino acids, phytol, and lysine while 2-hydroxyglutarate dehydrogenase is exclusively involved in lysine degradation. Given that the chlorophyll breakdown intermediate phytanoyl-CoA accumulates dramatically both in knockout mutants of the ETF/ETFQO complex and of isovaleryl-CoA dehydrogenase following growth in extended dark periods we have investigated the direct importance of chlorophyll breakdown for the supply of carbon and electrons during this process. For this purpose we isolated three independent Arabidopsis (Arabidopsis thaliana) knockout mutants of phytanoyl-CoA 2-hydroxylase and grew them under the same extended darkness regime as previously used. Despite the fact that these mutants accumulated phytanoyl-CoA and also 2-hydroxyglutarate they exhibited no morphological changes in comparison to the other mutants previously characterized. These results are consistent with a single entry point of phytol breakdown into the ETF/ETFQO system and furthermore suggest that phytol is not primarily metabolized by this pathway. Furthermore analysis of isovaleryl-CoA dehydrogenase/2-hydroxyglutarate dehydrogenase double mutants generated here suggest that these two enzymes essentially account for the entire electron input via the ETF complex.

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Language(s): eng - English
 Dates: 2011-07-252011
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: ISI:000294491800005
DOI: 10.​1104/​pp.​111.​182188
ISSN: 1532-2548 (Electronic)0032-0889 (Linking)
URI: ://000294491800005http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3221279/pdf/55.pdf?tool=pmcentrez
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Title: Plant Physiology
  Other : Plant Physiol.
Source Genre: Journal
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Publ. Info: Bethesda, Md. : American Society of Plant Biologists
Pages: - Volume / Issue: 157 (1) Sequence Number: - Start / End Page: 55 - 69 Identifier: ISSN: 0032-0889
CoNE: http://pubman.mpdl.mpg.de/cone/journals/resource/991042744294438