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hal.structure.identifierLight Photosynthesis & Metabolism [Photosynthesis]
dc.contributor.authorDELL'AGLIO, Elisa
hal.structure.identifierLight Photosynthesis & Metabolism [Photosynthesis]
dc.contributor.authorGIUSTINI, Cécile
hal.structure.identifierEtude de la dynamique des protéomes [EDyP ]
dc.contributor.authorKRAUT, Alexandra
hal.structure.identifierEtude de la dynamique des protéomes [EDyP ]
dc.contributor.authorCOUTÉ, Yohann
hal.structure.identifierUniversità degli Studi di Milano = University of Milan [UNIMI]
dc.contributor.authorCOSTA, Alex
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorDECROS, Guillaume
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGIBON, Yves
hal.structure.identifierLaboratoire de Recherche en Sciences Végétales [LRSV]
dc.contributor.authorMAZARS, Christian
hal.structure.identifierLight Photosynthesis & Metabolism [Photosynthesis]
dc.contributor.authorMATRINGE, Michel
hal.structure.identifierLight Photosynthesis & Metabolism [Photosynthesis]
dc.contributor.authorFINAZZI, Giovanni
hal.structure.identifierLight Photosynthesis & Metabolism [Photosynthesis]
dc.contributor.authorCURIEN, Gilles
dc.date.issued2019-09-14
dc.identifier.issn0032-0889
dc.description.abstractEn17 NADP(H) is an essential cofactor of multiple metabolic processes in all living organisms. In plants, 18 NADP(H) is required as the substrate of Ca 2+-dependent NADPH oxidases which catalyze a reactive 19 oxygen species burst in response to various stimuli. While NADP + production in plants has long been 20 known to involve a Calmodulin and Calcium (CaM)/Ca 2+-dependent NAD + kinase, the nature of the 21 enzyme catalyzing this activity has remained enigmatic, as well as its role in plant physiology. Here, 22 thanks to a combination of proteomics, biochemistry, molecular biology and in vivo studies, we have 23 identified an Arabidopsis protein that catalyzes NADP + production exclusively in the presence of 24 CaM/Ca 2+. This new enzyme (NADKc) has a CaM-binding peptide located in its N-terminal region and 25 displays peculiar biochemical properties as well as different domain organization compared to known 26 plant NAD + kinases. In response to a pathogen elicitor, activity of NADKc, which is associated with the 27 mitochondrial periphery, contributes to an increase in the cellular NADP + concentration and to the 28 amplification of the elicitor-induced oxidative burst. Based on a phylogenetic analysis and enzymatic 29 assays, we propose that the CaM/Ca 2+-dependent NAD + kinase activity found in photosynthetic 30
dc.description.sponsorshipMediterranean Center for Environment and Biodiversity - ANR-10-LABX-0004
dc.description.sponsorshipInfrastructure Française de Protéomique - ANR-10-INBS-0008
dc.language.isoen
dc.publisherOxford University Press ; American Society of Plant Biologists
dc.title.enIdentification of the Arabidopsis calmodulin-dependent NAD+ kinase that sustains the elicitor-induced oxidative burst
dc.typeArticle de revue
dc.identifier.doi10.1104/pp.19.00912
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
bordeaux.journalPlant Physiology
bordeaux.page1449-1458
bordeaux.volume181
bordeaux.issue4
bordeaux.peerReviewedoui
hal.identifierhal-02361156
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02361156v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Plant%20Physiology&rft.date=2019-09-14&rft.volume=181&rft.issue=4&rft.spage=1449-1458&rft.epage=1449-1458&rft.eissn=0032-0889&rft.issn=0032-0889&rft.au=DELL'AGLIO,%20Elisa&GIUSTINI,%20C%C3%A9cile&KRAUT,%20Alexandra&COUT%C3%89,%20Yohann&COSTA,%20Alex&rft.genre=article


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