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<dc:title xml:lang="fr">Caractérisation de l’attachement du mitoribosome à la membrane interne des mitochondries chez les plantes terrestres</dc:title>
<dcterms:alternative xml:lang="en">Characterization of mitoribosome tethering to the inner membrane of mitochondria in land plants</dcterms:alternative>
<dc:subject xml:lang="fr">Oxa1a</dc:subject>
<dc:subject xml:lang="fr">Mitochondrie</dc:subject>
<dc:subject xml:lang="fr">Traduction</dc:subject>
<dc:subject xml:lang="fr">Mitoribosome</dc:subject>
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<dcterms:abstract xml:lang="fr">Les ribosomes sont les complexes moléculaires responsables de la traduction de l’information génétique véhiculée par l’ARNm en protéines. La traduction cytosolique est bien caractérisée, contrairement à la traduction mitochondriale. Chez l’Homme et la levure, la traduction mitochondriale se déroule à la surface de la membrane interne de la mitochondrie de manière concomitante avec l’insertion des protéines néosynthétisées dans la membrane. Les mitoribosomes sont attachés directement à l’insertase Oxa1 par des mécanismes différents selon les groupes d’organismes. Chez les plantes terrestres, cette interaction n’a pas encore été observée et le mécanisme de l’interaction reste inconnu. Mes travaux se concentrent sur la caractérisation de l’interaction entre le mitoribosome de plante et l’insertase Oxa1a dans la membrane interne mitochondriale. Globalement, mes résultats ont montré qu’il existe une interaction directe entre le domaine C-ter d’Oxa1a (RBD) et une protéine constitutive du mitoribosome. Des expériences complémentaires de cryo-EM et de cryo-ET permettront de connaitre le site de contact exact et la ou les protéine(s) du mitoribosome responsable(s) de l’interaction avec Oxa1a.</dcterms:abstract>
<dcterms:abstract xml:lang="en">Ribosomes are the molecular complexes responsible for the translation of genetic information carried by mRNA into proteins. Cytosolic translation is well characterized unlike mitochondrial translation in eukaryotes. In humans and yeast, mitochondrial translation takes place on the surface of the inner membrane of the mitochondrion concomitantly with the insertion of neosynthesized proteins into the membrane. Mitoribosomes are attached directly to the Oxa1 insertase by different mechanisms in each group of organisms. In land plants, this interaction has not yet been observed and the interaction mechanism remains unknown. My work focuses on characterizing the interaction between the plant mitoribosome and the Oxa1a insertase in the mitochondrial inner membrane. Overall, my results showed that there is a direct interaction between the C-ter domain of Oxa1a (RBD) and a constitutive protein of the mitoribosome. Further cryo-EM and cryo-ET experiments will allow to know the exact contact site and the mitoribosome protein(s) responsible for the interaction with Oxa1a.</dcterms:abstract>
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