Structural basis of early translocation events on the ribosome

Peptide-chain elongation during protein synthesis entails sequential aminoacyl-tRNA selection and translocation reactions that proceed rapidly (2-20 per second) and with a low error rate (around 10(-3) to 10(-5) at each step) over thousands of cycles(1). The cadence and fidelity of ribosome transit through mRNA templates in discrete codon increments is a paradigm for movement in biological systems that must hold for diverse mRNA and tRNA substrates across domains of life. Here we use single-molecule fluorescence methods to guide the capture of structures of early translocation events on the bacterial ribosome. Our findings reveal that the bacterial GTPase elongation factor G specifically engages spontaneously achieved ribosome conformations while in an active, GTP-bound conformation to unlock and initiate peptidyl-tRNA translocation. These findings suggest that processes intrinsic to the pre-translocation ribosome complex can regulate the rate of protein synthesis, and that energy expenditure is used later in the translocation mechanism than previously proposed.

Automated summary

Research has shown that the bacterial GTPase elongation factor G specifically engages ribosome conformations achieved spontaneously in an active, GTP-bound state to facilitate translocation reactions. These findings suggest that processes intrinsic to the ribosome complex may regulate protein synthesis rates, with energy expenditure occurring later in the translocation mechanism than previously proposed.