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Margot Loussouarn-Yvon Le 07 Novembre 2017

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Margot Loussouarn-Yvon Le 07 Novembre 2017 AIX-MARSEILLE UNIVERSITE Ecole Doctorale des Sciences de la Vie et de la Santé (ED SVS 62) THESE pour obtenir le grade de DOCTEUR D’AIX-MARSEILLE UNIVERSITE EN BIOLOGIE VEGETALE Présentée et soutenue publiquement par Margot Loussouarn-Yvon Le 07 novembre 2017 L'ACIDE CARNOSIQUE ET LE CARNOSOL, DEUX SUPER-ANTIOXYDANTS DU ROMARIN (ROSMARINUS OFFICINALIS) Rôles, mécanismes, physiologie et applications Laboratoire d’Ecophysiologie Moléculaire des Plantes DSV/BIAM/LEMP, UMR 7265 CNRS/CEA/AMU CEA Cadarache Composition du jury: Alain Tissier, Professeur, Leibniz-Institute of Plant Biochemistry, Halle Rapporteur Laurent Urban, Professeur, Université d’Avignon et du Pays du Vaucluse Rapporteur Stefano Caffarri, Professeur, Université d’Aix-Marseille Président Michel Havaux, Directeur de Recherche, CEA Directeur de thèse Simona Birtić, Docteur, Naturex Co-encadrante de thèse Christophe Bailly, Professeur, Université Pierre et Marie Curie Examinateur Marie-Elisabeth Cuvelier, Docteur, INRA-Agroparistech Examinatrice Remerciements : Tout d’abord, je souhaite exprimer ma gratitude aux membres du jury pour l’évaluation de ce travail, notamment au Professeur Laurent Urban et au Professeur Alain Tissier pour avoir accepté d’en être les rapporteurs. Je remercie le Docteur Stefano Caffarri de bien vouloir présider le jury ainsi que le Professeur Christophe Bailly et au Docteur Marie-Elisabeth Cuvelier pour leur participation à ce jury. J’adresse également mes remerciements aux Docteurs Antoine Bily et Simona Birtić de la société Naturex de m’avoir fait confiance pendant ses 3 années pour mener à bien le sujet de thèse qu’ils m’ont proposé. Je remercie Simona Birtić en particulier pour ses conseils et son investissement quand j’en ai eu besoin. Je souhaite remercier particulièrement le Docteur Michel Havaux, directeur du laboratoire et directeur de ma thèse, pour son accueil, son encadrement, son investissement et ses conseils précieux. Je le remercie également pour sa capacité à prendre du recul et à répondre de manière perspicace aux questions posées, qu’elles soient scientifiques, professionnelles ou personnelles. Au-delà d’un excellent directeur de thèse, je suis heureuse d’avoir rencontré une personne avec de grande qualité humaine qui a su être à l’écoute lors d’épisode personnel douloureux. Je tiens également à remercier les personnes qui ont participé à ce projet. J’aimerais remercier le Professeur Anja Krieger-Liszkay pour m’avoir accueillie à plusieurs reprises dans son laboratoire, formée et conseillée sur les expériences de RPE. Je remercie aussi l’ingénieure Ljubica Svilar de la plateforme CRIBIOM pour son aide et son accompagnement lors des expériences de spectrométrie de masse. Je remercie toute l’équipe du GRAP (Groupe de Recherche Appliquée en Phytotechnologie) pour ses compétences techniques, et en particulier Patrice Ruellan, Frederic Espanet et Anne-Laure Benoit pour leur soutien dans les moments difficiles et pour les moments de détentes passés en leur compagnie. Je tiens à remercier chaleureusement Brigitte Ksas pour m’avoir formée aux différentes extractions et techniques HPLC du laboratoire, et surtout, je la remercie pour tous les moments agréables passés avec elle, son soutien, ses conseils et ce qu’elle est (si elle n’existait pas, il aurait fallu l’inventer). J’adresse également un très grand Merci aux étudiants du service, avec un spécial big-up à Fred, Louis, Ivana et Inès pour les rires, l’écoute, les sorties au grand air, les soirées Games of Thrones, les discussions philosophico-scientifiques de comptoirs et pour tous les moments doux et sincères passés ensemble. Ils ont été une réelle soupape de sécurité pour moi. J’ai aussi une pensée d’amitié pour Léo et Anne qui ont suivi de près mes débuts à Cadarache et avec qui j’ai passé des moments inoubliables. En guest-star, je voudrais remercier ma meilleure amie, Alix Richard, Docteur en bien-vivre, qui me soutient depuis 18 ans dans tout ce que j’entreprends et qui a toujours cru en moi (vive le fromage, la tisane et les lits !). Avec beaucoup d’amour, je dis un grand Merci à Gabriel et à ma grande famille pour m’avoir accompagnée et supportée ces derniers mois ardus. Ils sont contents que ce cycle se termine pour qu’un nouveau redémarre, et moi aussi. Je tiens également à transmettre ma gratitude à mes chats, Misépé, Patafoin et Snooky qui m’ont donné tellement d’amour dans les moments de solitude. Enfin, je dédie cette thèse à mon grand-père, le Professeur André Roux, qui a insufflé le goût de la science à ma famille et à moi-même ; et à mon grand frère Sébastien, passionné de la nature à toutes les échelles, sans qui, je n’aurais pas fait de biologie. Abréviations : 15-HEDE Acide 15-hydroxy-11,13 (Z,E)-eicosadienoique ABA Acide abscissique ADN Acide désoxyribonucléique ADNc AND complémentaire ADP Adénosine di-phosphate AE Acerola extract (actarit d’acérola) AGPI Acide gras polyinsaturé AIA Acide indole acétique AOX Alternative oxydase APX Ascorbate peroxydase ARN Acide ribonucléique ATP Adénosine tri-phosphate BET Bromure d’éthidium BHA Butylated hydroxyanisole BHT Butylated hydroxytoluene CA Carnosic acid (Acide carnosique) CARN Carnosol CAT Catalase CCD Charge coupled-device Col-0 Type sauvage columbia CPS Copalyl phosphate synthase CYP7/CYP8 Cytochrome P450 Cys Cystéine DGDG Digalactosyl diacyl glycérol DHA/MDHA Déhydroascorbate/Monodéhydroascorbate DHAR/MDHAR Déhydroascorbate réductase/Monodéhydroascorbate réductase dNTP Désoxyribonucléotides triphosphate DPPH 2,2-Diphenyl-1-picrylhydrazyl DTT Dithiothréitol EDTA Acide éthylène-diamine-tétraacétique ERE Espèces réactives électrophiles ERO Espèces réactives de l’oxygène FADH2/FAD Flavine adénine dinucléotide réduite/oxydée Fd Ferrédoxine FNR Ferrédoxine-NADP+ oxydoréductase FS Ferruginol synthase GAL l-Galactone-γ-lactone déshydrogénase GGDP Géranylgéranyl diphosphate GPX Glutathion peroxydase GR Glutathion réductase GSH/GSSG Glutathion réduit/oxydé HFS Hydroxyferruginol synthase HNE 4-hydroxy-2-nonenal HODE Acide octadécadiénoique HOTE Acide hydroxy octadécatriénoique HPLC-UV High performance liquid chromatography LA Linolenic acid LC-MS Liquid chromatography-mass spectrometry LHC Light harvesting complexe (antennes collectrices de lumière) MAPK Mitogen-activated proteine kinase MDA Malondialdéhyde MEBE Microscope électronique à balayage environnemental Met Méthionine MGDG Monogalactosyl diacyl glycérol MiS Miltiradiène synthase MSR Méthionine sulfoxide réductase MyoG Myoglobine G NAD(H) Nicotinamide adenine dinucleotide (réduit) NADP(H) Nicotinamide adenine dinucleotide phosphate (réduit) NCED 9-cis-epoxycarotenoide dismutase NPQ Non-photochemical quenching (piégeage non photochimique) OA/OSR Cocktails d’extraits végétaux enrichi en extrait de romarin PC/PC-OH Plastochromanol réduit/oxydé PCR Polymerase chain reaction PE Promegranate extract (extrait de grenade) PMSF Phenyl methylsulfonyl POBN 4-pyridyl-1-oxyde-N-tert-butylnitrone PQH2/PQ Plastoquinone réduite/oxydée PRX Peroxyrédoxine PSI/PSII Photosystème I/photosystème II qPCR Quantitative PCR RE Rosemary extract (extrait de romarin) RMN Résonance magnétique nucléaire RPE Résonance paramagnétique électronique RT Reverse transcriptase RubisCO Ribulose-1,5-biphosphate carboxylase/oxygénase SC Stabilisateur classique SOD Superoxyde dismutase SOSG Singlet oxygen sensor green SRX Sulfirédoxine TEMPD 2,2,6,6-tetraméthyl-4-pipéridone hydrochloride TOC Tocophérol TRX Thiorédoxine UPLC-MS Ultra-performance liquid chromatography-mass spectrometry XOD Xanthine oxydase SOMMAIRE : I. Synthèse bibliographique ........................................................................ - 1 - 1. La production d’espèces réactives de l’oxygène (ERO) ............................................. - 3 - 1.1. L’oxygène singulet .......................................................................................................... - 3 - 1.2. Le radical superoxyde ..................................................................................................... - 4 - 1.3. Le peroxyde d’hydrogène ............................................................................................... - 4 - 1.4. Le radical hydroxyle ....................................................................................................... - 5 - 2. Les sites de production des ERO ................................................................................ - 5 - 2.1. Les sites majoritaires de production des ERO ................................................................ - 5 - 2.1.1. Les mitochondries ................................................................................................... - 5 - 2.1.2. Les peroxysomes ..................................................................................................... - 7 - 2.1.3. Les chloroplastes ..................................................................................................... - 8 - 2.2. Les sites secondaires de production des ERO ................................................................. - 9 - 3. Les cibles macromoléculaires des ERO .................................................................... - 10 - 3.1. Les lipides ..................................................................................................................... - 10 - 3.2. Les protéines ................................................................................................................. - 13 - 3.3. Les acides nucléiques ...................................................................................................
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