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Hello darkness, my old friend: 3-KETOACYL-COENZYME A SYNTHASE4 is a branch point in the regulation of triacylglycerol synthesis in Arabidopsis thaliana

dc.rights.licenseopenen_US
hal.structure.identifierDepartment of Molecular Physiology [Potsdam-Golm]
hal.structure.identifierBen-Gurion University of the Negev [BGU]
dc.contributor.authorLUZAROWSKA, Urszula
dc.contributor.authorRUSS, Anne-Kathrin
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorJOUBÈS, Jérôme
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorBATSALE, Marguerite
dc.contributor.authorSZYMAŃSKI, Jędrzej
dc.contributor.authorP. THIRUMALAIKUMAR, Venkatesh
hal.structure.identifierDepartment of Molecular Physiology [Potsdam-Golm]
dc.contributor.authorLUZAROWSKI, Marcin
dc.contributor.authorWU, Si
hal.structure.identifierUniversity of British Columbia [Vancouver]
dc.contributor.authorZHU, Feng
hal.structure.identifierCharité - UniversitätsMedizin = Charité - University Hospital [Berlin]
dc.contributor.authorENDRES, Niklas
dc.contributor.authorKHEDHAYIR, Sarah
hal.structure.identifierHumboldt State University [HSU]
dc.contributor.authorSCHUMACHER, Julia
dc.contributor.authorJASINSKA, Weronika
hal.structure.identifierUniversity of California [Berkeley] [UC Berkeley]
dc.contributor.authorXU, Ke
hal.structure.identifierMax-Planck-Institut für Molekulare Pflanzenphysiologie [MPI-MP]
dc.contributor.authorCORREA CORDOBA, Sandra Marcela
dc.contributor.authorWEIL, Simy
hal.structure.identifierMax-Planck-Institut für Molekulare Pflanzenphysiologie [MPI-MP]
dc.contributor.authorSKIRYCZ, Aleksandra
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
hal.structure.identifierCenter of Plant Systems Biology and Biotechnology [Plovdiv] [CPSBB]
dc.contributor.authorFERNIE, Alisdair Robert
hal.structure.identifierInstitut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) [BIAM]
hal.structure.identifierEnvironnement, Bioénergie, Microalgues et Plantes [EBMP]
dc.contributor.authorLI-BEISSON, Yonghua
hal.structure.identifierUniversidad Nacional de Rosario [Santa Fe]
dc.contributor.authorFUSARI, Corina
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorBROTMAN, Yariv
dc.date.accessioned2024-04-30T11:48:35Z
dc.date.available2024-04-30T11:48:35Z
dc.date.issued2023-06-29
dc.identifier.issn1040-4651en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199540
dc.description.abstractEnAbstract Plant lipids are important as alternative sources of carbon and energy when sugars or starch are limited. Here, we applied combined heat and darkness or extended darkness to a panel of ∼300 Arabidopsis (Arabidopsis thaliana) accessions to study lipid remodeling under carbon starvation. Natural allelic variation at 3-KETOACYL-COENZYME A SYNTHASE4 (KCS4), a gene encoding an enzyme involved in very long chain fatty acid (VLCFA) synthesis, underlies the differential accumulation of polyunsaturated triacylglycerols (puTAGs) under stress. Ectopic expression of KCS4 in yeast and plants proved that KCS4 is a functional enzyme localized in the endoplasmic reticulum with specificity for C22 and C24 saturated acyl-CoA. Allelic mutants and transient overexpression in planta revealed the differential role of KCS4 alleles in VLCFA synthesis and leaf wax coverage, puTAG accumulation, and biomass. Moreover, the region harboring KCS4 is under high selective pressure and allelic variation at KCS4 correlates with environmental parameters from the locales of Arabidopsis accessions. Our results provide evidence that KCS4 plays a decisive role in the subsequent fate of fatty acids released from chloroplast membrane lipids under carbon starvation. This work sheds light on both plant response mechanisms and the evolutionary events shaping the lipidome under carbon starvation.
dc.language.isoENen_US
dc.title.enHello darkness, my old friend: 3-KETOACYL-COENZYME A SYNTHASE4 is a branch point in the regulation of triacylglycerol synthesis in Arabidopsis thaliana
dc.typeArticle de revueen_US
dc.identifier.doi10.1093/plcell/koad059en_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaireen_US
bordeaux.journalThe Plant cellen_US
bordeaux.page1984-2005en_US
bordeaux.volume35en_US
bordeaux.hal.laboratoriesLaboratoire de Biogenèse Membranaire (LBM) - UMR 5200en_US
bordeaux.issue6en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-04447661
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=The%20Plant%20cell&rft.date=2023-06-29&rft.volume=35&rft.issue=6&rft.spage=1984-2005&rft.epage=1984-2005&rft.eissn=1040-4651&rft.issn=1040-4651&rft.au=LUZAROWSKA,%20Urszula&RUSS,%20Anne-Kathrin&JOUB%C3%88S,%20J%C3%A9r%C3%B4me&BATSALE,%20Marguerite&SZYMA%C5%83SKI,%20J%C4%99drzej&rft.genre=article


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