Cover Feature: Allosteric Effects of EF-G Domain I Mutations Inducing Ribosome Frameshifting Revealed by Multiplexed Force Spectroscopy (ChemBioChem 19/2024)

Abstract

Ribosomal translocation, catalyzed by elongation factor G (EF-G), is a critical step in protein synthesis during which the ribosome typically moves three nucleotides along the mRNA per cycle. Using a new technique of multiplexed super-resolution force spectroscopy, it is shown that two engineered EF-G mutants, with mutated residues located approximately 80 Angstroms away from the EF-G pivot point, induce the ribosome to translocate by only two nucleotides, resulting in “-1” frameshifting. The article 10.1002/cbic.202400130 by Shoujun Xu, Yuhong Wang, and provides unique insights into EF-G-catalyzed ribosomal motion with single-nucleotide resolution from both ends of the mRNA.