期刊论文详细信息
Structural basis of early translocation events on the ribosome | |
Article | |
关键词: ELONGATION-FACTOR G; TRANSFER-RNA; EF-G; HYBRID STATE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; TRANSLATION; DYNAMICS; GTP; SELECTION; | |
DOI : 10.1038/s41586-021-03713-x | |
来源: SCIE |
【 摘 要 】
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.【 授权许可】
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