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hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorHOOKS, Mark
hal.structure.identifierUniversity of Manchester [Manchester]
dc.contributor.authorALLWOOD, J. William
hal.structure.identifierJohn Innes Centre [Norwich]
hal.structure.identifierUniversity of East Anglia [Norwich] [UEA]
dc.contributor.authorHARRISON, Joanna K. D.
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorKOPKA, Joachim
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorERBAN, Alexander
hal.structure.identifierUniversity of Manchester [Manchester]
dc.contributor.authorGOODACRE, Royston
hal.structure.identifierJohn Innes Centre [Norwich]
hal.structure.identifierUniversity of East Anglia [Norwich] [UEA]
dc.contributor.authorBALK, Janneke
dc.date.issued2014
dc.identifier.issn0264-6021
dc.description.abstractEnArabidopsis thaliana has three genes that encode distinct aconitases (ACO), but little is known about the function of each isoenzyme during plant development. In newly emerged seedlings of Arabidopsis, transcript and protein levels for ACO3 were selectively induced to yield more than 80% of total aconitase activity. Characterization of knockout mutants for each of the three ACOs suggests a major role for only ACO3 in citrate metabolism. The aco3 mutant showed delayed early seedling growth, altered assimilation of [C-14]acetate feeding and elevated citrate levels, which were nearly 4-fold greater than in wild-type, aco1 or aco2. However, both ACO1 and ACO2 are active in seedlings as shown by inhibition of aco3 growth by the toxin monofluoroacetate, and altered [C-14]acetate assimilation and metabolite levels in aco1 and aco2. Relative levels of fumarate and malate differed between aco2 and aco3, indicating metabolically isolated pools of these metabolites in seedlings. Our inability to enrich ACO protein through mitochondria isolation, and the reduced cytosolic ACO activity of the iron sulfur centre assembly mutant atm3-1, indicated a cytosolic localization of ACO3 in 3-day-old seedlings. Subsequently, we determined that more than 90% of ACO3 was cytosolic. We conclude that ACO3 is cytosolic in young seedlings and functions in citrate catabolism consistent with the operation of the classic glyoxylate and not direct catabolism of citrate within mitochondria.
dc.language.isoen
dc.publisherPortland Press
dc.subjectmitochondrion
dc.subject.encytosol
dc.subject.englyoxylate cycle
dc.subject.englyoxysome
dc.subject.enseedling
dc.title.enSelective induction and subcellular distribution of ACONITASE 3 reveal the importance of cytosolic citrate metabolism during lipid mobilization in <em>Arabidopsis</em>
dc.typeArticle de revue
dc.identifier.doi10.1042/BJ20140430
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale
bordeaux.journalBiochemical Journal
bordeaux.page309-317
bordeaux.volume463
bordeaux.issue2
bordeaux.peerReviewedoui
hal.identifierhal-02637096
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02637096v1
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