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Ewald R, Hoffmann C, Florian A, et al. Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis. Plant Physiol. 2014;165(3):978-990doi: 10.1104/pp.114.238311.
Ewald, R., Hoffmann, C., Florian, A., Neuhaus, E., Fernie, A. R., & Bauwe, H. (2014). Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis. Plant physiology, 165(3), 978-990. https://doi.org/10.1104/pp.114.238311
Ewald, Ralph, et al. "Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis." Plant physiology vol. 165,3 (2014): 978-990. doi: https://doi.org/10.1104/pp.114.238311
Ewald R, Hoffmann C, Florian A, Neuhaus E, Fernie AR, Bauwe H. Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis. Plant Physiol. 2014 Jul;165(3):978-990. doi: 10.1104/pp.114.238311. Epub 2014 May 28. PMID: 24872381; PMCID: PMC4081350.
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Plant Physiol. 2014 Jul;165(3):978-990. doi: 10.1104/pp.114.238311. Epub 2014 May 28.

Lipoate-Protein Ligase and Octanoyltransferase Are Essential for Protein Lipoylation in Mitochondria of Arabidopsis.

Plant physiology

Ralph Ewald, Christiane Hoffmann, Alexandra Florian, Ekkehard Neuhaus, Alisdair R Fernie, Hermann Bauwe

Affiliations

  1. Department of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.).
  2. Department of Plant Physiology, University of Rostock, D-18059 Rostock, Germany (R.E., H.B.);Department of Plant Physiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany (C.H., E.N.); andMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany (A.F., A.R.F.) [email protected].

PMID: 24872381 PMCID: PMC4081350 DOI: 10.1104/pp.114.238311

Abstract

Prosthetic lipoyl groups are required for the function of several essential multienzyme complexes, such as pyruvate dehydrogenase (PDH), α-ketoglutarate dehydrogenase (KGDH), and the glycine cleavage system (glycine decarboxylase [GDC]). How these proteins are lipoylated has been extensively studied in prokaryotes and yeast (Saccharomyces cerevisiae), but little is known for plants. We earlier reported that mitochondrial fatty acid synthesis by ketoacyl-acyl carrier protein synthase is not vital for protein lipoylation in Arabidopsis (Arabidopsis thaliana) and does not play a significant role in roots. Here, we identify Arabidopsis lipoate-protein ligase (AtLPLA) as an essential mitochondrial enzyme that uses octanoyl-nucleoside monophosphate and possibly other donor substrates for the octanoylation of mitochondrial PDH-E2 and GDC H-protein; it shows no reactivity with bacterial and possibly plant KGDH-E2. The octanoate-activating enzyme is unknown, but we assume that it uses octanoyl moieties provided by mitochondrial β-oxidation. AtLPLA is essential for the octanoylation of PDH-E2, whereas GDC H-protein can optionally also be octanoylated by octanoyltransferase (LIP2) using octanoyl chains provided by mitochondrial ketoacyl-acyl carrier protein synthase to meet the high lipoate requirement of leaf mesophyll mitochondria. Similar to protein lipoylation in yeast, LIP2 likely also transfers octanoyl groups attached to the H-protein to KGDH-E2 but not to PDH-E2, which is exclusively octanoylated by LPLA. We suggest that LPLA and LIP2 together provide a basal protein lipoylation network to plants that is similar to that in other eukaryotes.

© 2014 American Society of Plant Biologists. All Rights Reserved.

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