A thermal ratchet model of tRNA-mRNA translocation by the ribosome.
The translocation of tRNA coupled with mRNA in the ribosome is one of important steps during protein synthesis. Despite extensive experimental studies, the detailed mechanism of the translocation remains undetermined. Here, based on previous biochemical, cryo-electron microscopic and X-ray crystallographic studies, a thermal ratchet model is presented for this translocation. In the model, during one elongation cycle of the protein synthesis, two large conformational transitions of the ribosome are involved, with one being the relative rotation between the two ribosomal subunits following the peptide transfer, which is facilitated by the EF-G.GTP binding, and the other one being the reverse relative rotation between the two ribosomal subunits upon EF-G.GTP hydrolysis. The former conformational change plays an important role in ensuring the completion of the release of the deacylated tRNA from the ribosome before tRNA-mRNA translocation. The latter reverse conformational change upon GTP hydrolysis is followed by rapid tRNA-mRNA translocation and Pi release, both of which take place independently of each other. This is consistent with the previous biochemical experimental data. Also, the model is consistent with other available experimental results such as the suppression of EF-G-dependent translocation in cross-linked ribosomes and frameshifting under some conditions.
Xie
Ping
P
Institute of Physics, Chinese Academy of Sciences, Beijing, China. pxie@aphy.iphy.ac.cn
D003198:Computer Simulation; D006358:Hot Temperature; D008956:Models, Chemical; D008958:Models, Molecular; D009038:Motion; D021381:Protein Transport; D012333:RNA, Messenger / Q000737:chemistry* / Q000648:ultrastructure*; D012343:RNA, Transfer / Q000737:chemistry* / Q000648:ultrastructure*; D012270:Ribosomes / Q000737:chemistry* / Q000648:ultrastructure*; D013816:Thermodynamics
D012333:RNA, Messenger; D012343:RNA, Transfer