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<dc:title xml:lang="en">Study of the mitochondrial or vacuolar localization of multi-localized cytosolic aminoacyl-tRNA synthetases in the yeast Saccharomyces cerevisiae</dc:title>
<dcterms:alternative xml:lang="fr">Étude de la localisation mitochondriale ou vacuolaire d’aminoacyl-ARNt synthétases cytosoliques multi-localisées chez la levure Saccharomyces cerevisiae</dcterms:alternative>
<dc:subject xml:lang="fr">Aminoacyl-ARNt synthétase</dc:subject>
<dc:subject xml:lang="fr">S. cerevisiae</dc:subject>
<dc:subject xml:lang="fr">Échoformes</dc:subject>
<dc:subject xml:lang="fr">Mitochondrie</dc:subject>
<dc:subject xml:lang="fr">Vacuole</dc:subject>
<dc:subject xml:lang="fr">TORC1</dc:subject>
<dc:subject xml:lang="en">Aminoacyl-tRNA synthetase</dc:subject>
<dc:subject xml:lang="en">S. cerevisiae</dc:subject>
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<dcterms:abstract xml:lang="fr">Les aminoacyl-ARNt synthétases (aaRSs) catalysent la formation des aminoacyl-ARNt utilisés par la machinerie traductionnelle. La relocalisation subcellulaire de ces enzymes est souvent associée à des fonctions non-canoniques. La levure S. cerevisiae contient un complexe multisynthétasique, appelé complexe AME, composé de la méthionyl- et de la glutamyl-ARNt synthétases (MRS et ERS) et du cofacteur Arc1. Bien que le complexe ait été décrit comme exclusivement cytosolique, les deux aaRSs peuvent se relocaliser dans différents compartiments subcellulaires. On parle alors d’échoformes cytosoliques et organellaires. De plus, Arc1 interagit avec des lipides vacuolaires in vitro, suggérant une localisation vacuolaire in vivo. Pour identifier les échoformes mitochondriales et vacuolaires (vace) de protéines cytosoliques, nous avons élaboré deux outils de microscopie à épifluorescence. Nous avons pu identifier une nouvelle échoforme mitochondriale pour deux aaRSs, ainsi que des échoformes vacuolaires pour toutes les aaRSs testées et pour les composants du complexe AME. Une potentielle implication de vaceMRS dans l’inhibition du complexe TORC1 vacuolaire a également été mise en évidence.</dcterms:abstract>
<dcterms:abstract xml:lang="en">The aminoacyl-tRNA synthetases (aaRSs) are responsible for the formation of aminoacyl-tRNAs used by the translational machinery. The subcellular relocalization of these proteins is often associated with non-canonical functions. The yeast S. cerevisiae contains a multisynthetasic complex, called AME complex, composed of the methionyl- and glutamyl-tRNA synthetases (MRS and ERS) and the cofactor Arc1. Even if the complex has been described as exclusively cytosolic, the two aaRSs can relocate in different subcellular compartments. These proteins are thus referred as cytosolic or organellar echoforms. Moreover, Arc1 interacts with vacuolar lipids in vitro, suggesting a vacuolar localization in vivo. To visualize mitochondrial and vacuolar (vace) echoforms of cytosolic proteins, we engineered two epifluorescence microscopy tools. We identified a new mitochondrial echoform for two aaRSs, as well as vacuolar echoforms for all the cytosolic aaRSs tested and the AME components. A potential implication of vaceMRS in TORC1 inhibition was also observed.</dcterms:abstract>
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