title: Mitochondrial protein lipoylation does not exclusively depend on the mtKAS pathway of de novo fatty acid synthesis in Arabidopsis.
abstract: The photorespiratory Arabidopsis (Arabidopsis thaliana) mutant gld1 (now designated mtkas-1) is deficient in glycine decarboxylase (GDC) activity, but the exact nature of the genetic defect was not known. We have identified the mtkas-1 locus as gene At2g04540, which encodes beta-ketoacyl-[acyl carrier protein (ACP)] synthase (mtKAS), a key enzyme of the mitochondrial fatty acid synthetic system. One of its major products, octanoyl-ACP, is regarded as essential for the intramitochondrial lipoylation of several proteins including the H-protein subunit of GDC and the dihydrolipoamide acyltransferase (E2) subunits of two other essential multienzyme complexes, pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase. This view is in conflict with the fact that the mtkas-1 mutant and two allelic T-DNA knockout mutants grow well under nonphotorespiratory conditions. Although on a very low level, the mutants show residual lipoylation of H protein, indicating that the mutation does not lead to a full functional knockout of GDC. Lipoylation of the pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase E2 subunits is distinctly less reduced than that of H protein in leaves and remains unaffected from the mtKAS knockout in roots. These data suggest that mitochondrial protein lipoylation does not exclusively depend on the mtKAS pathway of lipoate biosynthesis in leaves and may occur independently of this pathway in roots.
authors.affiliation: Department of Plant Physiology, University of Rostock, D-18059 Rostock, Germany.
authors.forename: Ralph
authors.initials: R
authors.lastname: Ewald
authors.forename: Uner
authors.initials: U
authors.lastname: Kolukisaoglu
authors.forename: Ursula
authors.initials: U
authors.lastname: Bauwe
authors.forename: Stefan
authors.initials: S
authors.lastname: Mikkat
authors.forename: Hermann
authors.initials: H
authors.lastname: Bauwe
mesh_terms: D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000235:genetics / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D003653:Decarboxylation; D005227:Fatty Acids / Q000096:biosynthesis / Q000378:metabolism*; D016368:Frameshift Mutation; D005998:Glycine / Q000378:metabolism; D050961:Glycine Decarboxylase Complex H-Protein / Q000378:metabolism*; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins / Q000378:metabolism; D010788:Photosynthesis / Q000502:physiology; D018515:Plant Leaves / Q000378:metabolism; D018517:Plant Roots / Q000378:metabolism; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism
chemical_list: D000596:Amino Acids; D005227:Fatty Acids; D050961:Glycine Decarboxylase Complex H-Protein; D007527:Isoenzymes; D024101:Mitochondrial Proteins; D011768:Pyruvate Dehydrogenase Complex; D007655:Ketoglutarate Dehydrogenase Complex; C078182:beta-ketoacyl-acyl carrier protein synthase I; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; D005998:Glycine