Biologie Digitale de l’ARN

@article{,

title = {Structural insights into the role of diphthamide on elongation factor 2 in messenger RNA reading frame maintenance},

author = {S Pellegrino and N Demeshkina and E Mancera-Martinez and S Melnikov and A Simonetti and A Myasnikov and M Yusupov and G Yusupova and Y Hashem},

url = {https://www.ncbi.nlm.nih.gov/pubmed/29886014?dopt=Abstract},

doi = {10.1016/j.jmb.2018.06.006},

isbn = {29886014},

year  = {2018},

date = {2018-01-01},

journal = {J Mol Biol},

volume = {430},

number = {17},

pages = {2677-2687},

abstract = {One of the most critical steps of protein biosynthesis is the coupled movement of messenger RNA (mRNA), that encodes genetic information, with transfer RNAs (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-EM structures of yeast 80S ribosome complexes containing mRNA, tRNA and eEF2 trapped in different GTP-hydrolysis states which provide further structural insights on the role of diphthamide in the mechanism of translation fidelity in eukaryotes.},

keywords = {ENNIFAR, Ribosome translocation cryo-EM diphthamide eEF2 reading-frame maintenance, Unité ARN},

pubstate = {published},

tppubtype = {article}

}