Afficher la notice abrégée

Tackling functional redundancy of Arabidopsis fatty acid elongase complexes

hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorBATSALE, Marguerite
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorALONSO, Marie
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorPASCAL, Stéphanie
dc.contributor.authorTHORAVAL, Didier
hal.structure.identifierPlant Sciences, Rothamsted Research, Harpenden, United Kingdom
dc.contributor.authorHASLAM, Richard
hal.structure.identifierPlant Sciences, Rothamsted Research, Harpenden, United Kingdom
dc.contributor.authorBEAUDOIN, Frédéric
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorDOMERGUE, Frédéric
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorJOUBÈS, Jérôme
dc.date.issued2023-01-25
dc.identifier.issn1664-462X
dc.description.abstractEnVery-long-chain fatty acids (VLCFA) are precursors for various lipids playing important physiological and structural roles in plants. Throughout plant tissues, VLCFA are present in multiple lipid classes essential for membrane homeostasis, and also stored in triacylglycerols. VLCFA and their derivatives are also highly abundant in lipid barriers, such as cuticular waxes in aerial epidermal cells and suberin monomers in roots. VLCFA are produced by the fatty acid elongase (FAE), which is an integral endoplasmic reticulum membrane multi-enzymatic complex consisting of four core enzymes. The 3-ketoacyl-CoA synthase (KCS) catalyzes the first reaction of the elongation and determines the chain-length substrate specificity of each elongation cycle, whereas the other three enzymes have broad substrate specificities and are shared by all FAE complexes. Consistent with the co-existence of multiple FAE complexes, performing sequential and/or parallel reactions to produce the broad chain-length-range of VLCFA found in plants, twenty-one KCS genes have been identified in the genome of Arabidopsis thaliana . Using CRISPR-Cas9 technology, we established an expression platform to reconstitute the different Arabidopsis FAE complexes in yeast. The VLCFA produced in these yeast strains were analyzed in detail to characterize the substrate specificity of all KCS candidates. Additionally, Arabidopsis candidate proteins were transiently expressed in Nicotiana benthamiana leaves to explore their activity and localization in planta . This work sheds light on the genetic and biochemical redundancy of fatty acid elongation in plants.
dc.language.isoen
dc.publisherFrontiers
dc.title.enTackling functional redundancy of Arabidopsis fatty acid elongase complexes
dc.typeArticle de revue
dc.identifier.doi10.3389/fpls.2023.1107333
dc.subject.halSciences du Vivant [q-bio]
bordeaux.journalFrontiers in Plant Science
bordeaux.volume14
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionCNRS
hal.identifierhal-04254570
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-04254570v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Frontiers%20in%20Plant%20Science&rft.date=2023-01-25&rft.volume=14&rft.eissn=1664-462X&rft.issn=1664-462X&rft.au=BATSALE,%20Marguerite&ALONSO,%20Marie&PASCAL,%20St%C3%A9phanie&THORAVAL,%20Didier&HASLAM,%20Richard&rft.genre=article


Fichier(s) constituant ce document

FichiersTailleFormatVue

Il n'y a pas de fichiers associés à ce document.

Ce document figure dans la(les) collection(s) suivante(s)

Afficher la notice abrégée