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Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance

Lookup NU author(s): Dr Sergey MelnikovORCiD

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Abstract

© 2018 Elsevier LtdOne 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.

Publication metadata

Author(s): Pellegrino S, Demeshkina N, Mancera-Martinez E, Melnikov S, Simonetti A, Myasnikov A, Yusupov M, Yusupova G, Hashem Y

Publication type: Article

Publication status: Published

Journal: Journal of Molecular Biology

Year: 2018

Volume: 430

Issue: 17

Pages: 2677-2687

Print publication date: 17/08/2018

Online publication date: 07/06/2018

Acceptance date: 04/06/2018

ISSN (print): 0022-2836

ISSN (electronic): 1089-8638

Publisher: Academic Press

URL: https://doi.org/10.1016/j.jmb.2018.06.006

DOI: 10.1016/j.jmb.2018.06.006

PubMed id: 29886014

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