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S. Essentielle-chez, T. Oneidensis, and . Est-connue-pour-permettre-la-maturation-d-'un-arn-de-transfert, Par différentes approches, j'ai montré que (i) l'activité et la quantité de TilS sont réduites en absence d'Hsp90So, (ii) TilS et Hsp90So interagissent et (iii) Hsp90So empêche l'agrégation de la protéine TilS in vitro. Ces résultats montrent que TilS est une nouvelle protéine cliente de Hsp90So. Enfin, je me suis intéressée à la protéine YbbN de S. oneidensis dont la séquence codante est proche du gène hsp90. YbbN est décrite pour avoir une fonction chaperon chez d'autres bactéries. Mes résultats préliminaires montrent que Hsp90So et YbbN interagissent, ce qui suggère l'existence d'une collaboration entre les deux protéines. Des études supplémentaires seront nécessaires pour une meilleure compréhension du rôle de YbbN chez cette bactérie. En conclusion