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

https://www.ncbi.nlm.nih.gov/pubmed/29886014

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.