Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance.
Fiche publication
Date publication
août 2018
Journal
Journal of molecular biology
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat, Dr YUSUPOVA Gulnara, Dr SIMONETTI Angelita
Tous les auteurs :
Pellegrino S, Demeshkina N, Mancera-Martinez E, Melnikov S, Simonetti A, Myasnikov A, Yusupov M, Yusupova G, Hashem Y
Lien Pubmed
Résumé
One of the most critical steps of protein biosynthesis is the coupled movement of mRNA, which encodes genetic information, with tRNAs on the ribosome. In eukaryotes, this process is catalyzed by a conserved G-protein, the elongation factor 2 (eEF2), which carries a unique post-translational modification, called diphthamide, found in all eukaryotic species. Here we present near-atomic resolution cryo-electron microscopy structures of yeast 80S ribosome complexes containing mRNA, tRNA and eEF2 trapped in different GTP-hydrolysis states which provide further structural insights into the role of diphthamide in the mechanism of translation fidelity in eukaryotes.
Mots clés
cryo-EM, diphthamide, eEF2, reading-frame maintenance, ribosome translocation
Référence
J. Mol. Biol.. 2018 Aug 17;430(17):2677-2687