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PMID: 21788362 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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 ·Vol. 157 ·No. 1 ·2011-09-00 ·Pages 55-69

Araújo WL, Ishizaki K, Nunes-Nesi A, Tohge T, Larson TR, Krahnert I, Balbo I, Witt S, Dörmann P, Graham IA, Leaver CJ, Fernie AR

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.

MeSH Terms
Amino Acids/metabolism Arabidopsis/enzymology Coenzyme A/genetics,metabolism Darkness Electron-Transferring Flavoproteins/metabolism Mutation Oxidoreductases/metabolism Phytanic Acid/analogs & derivatives,metabolism Ubiquitin/metabolism
Chemicals
Amino Acids Electron-Transferring Flavoproteins Ubiquitin phytanoyl-coenzyme A Phytanic Acid Oxidoreductases Coenzyme A
Authors & Affiliations
12 authors, click to expand affiliations / ORCID
Araújo Wagner L
Max Planck Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany.
Ishizaki Kimitsune
Nunes-Nesi Adriano
Tohge Takayuki
Larson Tony R
Krahnert Ina
Balbo Ilse
Witt Sandra
Dörmann Peter
Graham Ian A
Leaver Christopher J
Fernie Alisdair R
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Article Info
Journal
Plant physiology
Abbr.
Plant Physiol
ISSN
1532-2548
Published
2011-09-00
Epub
2011-00-25
Pages
55-69
Language
English
Region
United States
NLM ID
0401224
PMCID
PMC3221279
Subset
IM
Grants
Biotechnology and Biological Sciences Research Council · United Kingdom
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