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Etudes structurales et fonctionnelles de complexes entre Trm112 et différentes méthyltransférases impliquées dans la traduction

Abstract : Protein synthesis is a central process in the cell; it ensures the transfer of genetic information from mRNA in to protein. A lot of actors are involved directly or indirectly in translation. In Eukaryotes, Trm112, a small protein, interacts with and activates four methyltransferases modifying direct actors of translation. The termination factor eRF1 is methylated by the Mtq2-Trm112 complex, the 18S rRNA by Bud23-Trm112 and some tRNA by the Trm9-Trm112 and Trm11-Trm112 complexes. During this work, the crystal structures of Trm9-Trm112 and Bud23-Trm112 complexes from yeast were solved. The comparative analysis of these two new structures with Mtq2-Trm112 structure highlights the structural plasticity allowing Trm112 to interact through a very similar mode with its partners although those share less than 20% sequence identity. In the same organism, the key residues for the interaction with Trm112 are conserved or share similar characteristics. In addition to the structural analysis, the function of the Trm9-Trm112 complex was studied in S. cerevisiae. This analysis allowed to map the active site of the enzyme and to propose a model of its mechanism of action. Finally, the first data obtained in vivo, with the Archaea Haloferax volcanii suggest that the Trm112 platform might also be present in some prokaryotic organisms.
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Submitted on : Friday, July 20, 2018 - 3:27:07 PM
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Juliette Létoquart. Etudes structurales et fonctionnelles de complexes entre Trm112 et différentes méthyltransférases impliquées dans la traduction. Biochimie [q-bio.BM]. Université Paris Sud - Paris XI, 2014. Français. ⟨NNT : 2014PA114821⟩. ⟨tel-01845687⟩

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