The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Identification of the 2-Hydroxyglutarate and Isovaleryl-CoA Dehydrogenases as Alternative Electron Donors Linking Lysine Catabolism to the Electron Transport Chain of Arabidopsis Mitochondria
Open accessAbstract
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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Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
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GMD@CSB.DB: the Golm Metabolome Database
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Self-citationGABA in plants: just a metabolite?
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Protein degradation – an alternative respiratory substrate for stressed plants
Araújo, W. L., Tohge, T., Ishizaki, K., Leaver, C. J., & Fernie, A. R. (2011) · Trends in Plant Science · doi:10.1016/j.tplants.2011.05.008 · Cited by 438
Self-citationThe Regulation of Essential Amino Acid Synthesis and Accumulation in Plants
Galili, G., Amir, R., & Fernie, A. R. (2016) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-043015-112213 · Cited by 422
Self-citationAutophagy, plant senescence, and nutrient recycling
Avila-Ospina, L., Moison, M., Yoshimoto, K., & Masclaux-Daubresse, C. (2014) · Journal of Experimental Botany · doi:10.1093/jxb/eru039 · Cited by 369
Watanabe, M., Balazadeh, S., Tohge, T., Erban, A., Giavalisco, P., Kopka, J., Mueller-Roeber, B., Fernie, A. R., & Hoefgen, R. (2013) · Plant Physiology · doi:10.1104/pp.113.217380 · Cited by 320
Self-citationThe evolution of phenylpropanoid metabolism in the green lineage
Tohge, T., Watanabe, M., Hoefgen, R., & Fernie, A. R. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.758083 · Cited by 296
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Metadata
- Authors
- Araújo, W. L., Ishizaki, K., Nunes-Nesi, A., Larson, T. R., Tohge, T., Krahnert, I., Witt, S., Obata, T., Schauer, N., Graham, I. A., Leaver, C. J., & Fernie, A. R.
- Venue
- The Plant Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-05-01
- Volume
- 22
- Issue
- 5
- Pages
- 1549-1563
- ISSN
- 1040-4651 (ISSN-L)
- 1532-298X
- OpenAlex
- W2100999167
- Cited by
- 340
- References
- 51
- FWCI
- 6.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Araújo, W. L., Ishizaki, K., Nunes-Nesi, A., Larson, T. R., Tohge, T., Krahnert, I., Witt, S., Obata, T., Schauer, N., Graham, I. A., Leaver, C. J., & Fernie, A. R. (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. https://doi.org/10.1105/tpc.110.075630
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