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<dc:title xml:lang="fr">ARNt "manchots" : structure, fonctionnalité et évolution</dc:title>
<dcterms:alternative xml:lang="en">Structure, function and evolution of armless mitochondrial tRNAs</dcterms:alternative>
<dc:subject xml:lang="fr">ARN transfert</dc:subject>
<dc:subject xml:lang="fr">Mitochondrie</dc:subject>
<dc:subject xml:lang="fr">CCAse</dc:subject>
<dc:subject xml:lang="fr">Aminoacyl-ARNt synthetase</dc:subject>
<dc:subject xml:lang="fr">Romanomermis culicivorax</dc:subject>
<dc:subject xml:lang="en">Transfer RNA</dc:subject>
<dc:subject xml:lang="en">Mitochondria</dc:subject>
<dc:subject xml:lang="en">CCA-adding enzyme</dc:subject>
<dc:subject xml:lang="en">Aminoacyl-tRNA synthetase</dc:subject>
<dc:subject xml:lang="en">Romanomermis culicivorax</dc:subject>
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<tef:elementdEntree autoriteExterne="033442207" autoriteSource="Sudoc">Aminoacyl-ARNt synthétases</tef:elementdEntree>
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<tef:elementdEntree autoriteExterne="031445551" autoriteSource="Sudoc">ARN de transfert</tef:elementdEntree>
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<dcterms:abstract xml:lang="fr">Les ARNt sont des molécules adaptatrices reliant l'information génétique de l’ARN messagers à la séquence d'acides aminés primaire des protéines. Les ARNt ont une structure typique, appelée "feuille de trèfle". Certains ARNt mitochondriaux montrent une forte dérivation de cette structure. Un cas extrême peut être observé dans les mitochondries du nématode R. culicivorax. Cette étude vise la caractérisation fonctionnelle de ces ARNt «bizarres» et de définir leurs propriétés structurales et leur fonctionnalité avec des protéines partenaires telles que les CCAses et les aminoacyl-ARNt synthetases. Ce travail révèle que les ARNt sans bras forment une structure secondaire en forme d'épingle à cheveux et que leurs structures 3D présentent une grande flexibilité intrinsèque. Les tests initiaux n’ont pas démontré l'activité d'aminoacylation. Cependant, les ARNt sans bras représentent des molécules fonctionnelles pour le CCAse, indiquant des adaptations de l’enzyme aux ARNt sans bras.</dcterms:abstract>
<dcterms:abstract xml:lang="en">TRNAs are adapter molecules linking the genetic information of messenger RNAs with the primary amino acid sequence of proteins. tRNAs have a typical cloverleaf-like secondary structure. Some mitochondrial tRNAs show a high derivation from this canonical tRNA structure. An extreme case of structural truncations can be observed in mitochondria of the nematode R. culicivorax. This study aims the functional characterization of such “bizarre” tRNAs in defining their structural properties and their functionality with interacting partner proteins such as CCA-adding enzymes and aminoacyl-tRNA synthetases. This work reveals that armless tRNAs form a hairpin-shaped secondary structure. 3D structures exhibit a high intrinsic flexibility. Initial tests could not demonstrate aminoacylation activity. However, armless tRNAs represent functional molecules for CCA-incorporation, indicating adaptations of CCA-adding enzymes to armless tRNAs.</dcterms:abstract>
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