Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP

Christine E. Carbone, Anna B. Loveland, Howard B. Gamper, Ya-Ming Hou, Gabriel Demo () and Andrei A. Korostelev ()
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Christine E. Carbone: UMass Chan Medical School
Anna B. Loveland: UMass Chan Medical School
Howard B. Gamper: Thomas Jefferson University
Ya-Ming Hou: Thomas Jefferson University
Gabriel Demo: UMass Chan Medical School
Andrei A. Korostelev: UMass Chan Medical School

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: Abstract During translation, a conserved GTPase elongation factor—EF-G in bacteria or eEF2 in eukaryotes—translocates tRNA and mRNA through the ribosome. EF-G has been proposed to act as a flexible motor that propels tRNA and mRNA movement, as a rigid pawl that biases unidirectional translocation resulting from ribosome rearrangements, or by various combinations of motor- and pawl-like mechanisms. Using time-resolved cryo-EM, we visualized GTP-catalyzed translocation without inhibitors, capturing elusive structures of ribosome•EF-G intermediates at near-atomic resolution. Prior to translocation, EF-G binds near peptidyl-tRNA, while the rotated 30S subunit stabilizes the EF-G GTPase center. Reverse 30S rotation releases Pi and translocates peptidyl-tRNA and EF-G by ~20 Å. An additional 4-Å translocation initiates EF-G dissociation from a transient ribosome state with highly swiveled 30S head. The structures visualize how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA-mRNA translocation, whereas GTP hydrolysis and Pi release drive EF-G dissociation.

Date: 2021
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DOI: 10.1038/s41467-021-27415-0

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