作者: L. H. Horan , H. F. Noller
关键词: Elongation factor 、 Biochemistry 、 Eukaryotic Ribosome 、 30S 、 Ribosome 、 Transfer RNA 、 Peptide Elongation Factor G 、 Biology 、 50S 、 Protein biosynthesis 、 Biophysics
摘要: Translocation of tRNA and mRNA during protein synthesis is believed to be coupled structural changes in the ribosome. The “ratchet model,” based on cryo-EM reconstructions ribosome complexes, invokes relative movement 30S 50S ribosomal subunits this process; however, evidence that directly demonstrates a requirement for intersubunit translocation lacking. To address problem, we created an disulfide cross-link restrict potential movement. cross-linked ribosomes were unable carry out polypeptide synthesis; inhibition was completely reversed upon reduction bridge. In vitro assays showed specifically blocked elongation factor G-dependent translocation. These findings show required translocation, accounting universal two-subunit architecture ribosomes.