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<dc:title xml:lang="fr">Rôle du facteur d'initiation eIF3 dans la traduction de l'ARNm de l'histone H4</dc:title>
<dcterms:alternative xml:lang="en">Rôle of the initiation factor eIF3 in the histone H4 mRNA translation</dcterms:alternative>
<dc:subject xml:lang="fr">ARNm d’histone H4</dc:subject>
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<dc:subject xml:lang="fr">Initiation de la traduction</dc:subject>
<dc:subject xml:lang="en">Histone H4 mRNA</dc:subject>
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<dc:subject xml:lang="en">Translation initiation</dc:subject>
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<tef:elementdEntree autoriteExterne="073295795" autoriteSource="Sudoc.FMesh">Facteur-3 d'initiation eucaryote</tef:elementdEntree>
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<dcterms:abstract xml:lang="fr">La traduction de l’ARNm de l’histone H4 est initiée par un mécanisme original combinant à la fois certaines caractéristiques canoniques (fixation à la coiffe) et virales (absence de scanning et entrée interne des ribosomes). Le facteur d’initiation eIF3, un complexe de 13 sous-unités (a-m), assure le recrutement sélectif d’ARNm cellulaires, dont celui de l’histone H4, afin de contrôler leur expression. Dans cette thèse nous avons démontré l’interaction entre le facteur eIF3 et les ARNm de H4 et des histones H1, H2A, H2B et H3 in vivo et identifié 4 sous-unités eIF3c, d, e et g en interaction avec l’ARNm H4. Celles-ci se lient aux ARNm d’histones in vitro indépendamment du complexe eIF3. Nous avons analysé le rôle fonctionnel d’eIF3 sur la synthèse des histones in vivo et montré que l’inhibition des 4 sous-unités par siARN augmente la traduction des histones au début de la phase S du cycle cellulaire. eIF3 semble réprimer la traduction des ARNm d’histones quand il n’est pas limitant.</dcterms:abstract>
<dcterms:abstract xml:lang="en">The translation of the histone H4 mRNA is initiated by an original mechanism that combines both canonical (binding to the cap) and viral (absence of scanning and internal entry of ribosomes) characteristics. The initiation factor eIF3, a complex of 13 subunits (a-m), selectively recruits cellular mRNAs, including histone H4, to control their expression. In this thesis we demonstrated the interaction between eIF3 and the mRNAs of H4 and histones H1, H2A, H2B and H3 in vivo and identified 4 subunits eIF3c, d, e and g in interaction with H4 mRNA. These subunits bind to histone mRNAs in vitro independently of the eIF3 complex. We analyzed the functional role of eIF3 on histone synthesis in vivo and showed that inhibition of the 4 subunits by siRNA increased histone translation at the beginning of the S phase of the cell cycle. eIF3 appears to suppress translation of histone mRNAs when it is not limiting.</dcterms:abstract>
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