期刊
STRUCTURE
卷 16, 期 5, 页码 664-672出版社
CELL PRESS
DOI: 10.1016/j.str.2008.04.001
关键词
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资金
- Biotechnology and Biological Sciences Research Council [BB/D009499/1, BB/D013305/1] Funding Source: researchfish
- Medical Research Council [G0500365] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/D013305/1, BB/D009499/1] Funding Source: Medline
- Medical Research Council [G0500365] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- BBSRC [BB/D009499/1, BB/D013305/1] Funding Source: UKRI
- MRC [G0500365] Funding Source: UKRI
The translation of genetic information into proteins is a fundamental process of life. Stepwise addition of amino acids to the growing polypeptide chain requires the coordinated movement of mRNA and tRNAs through the ribosome, a process known as translocation. Here, we review current understanding of the kinetics and mechanics of translocation, with particular emphasis on the structure of a functional mammalian ribosome stalled during translocation by an mRNA pseudoknot. In the context of a pseudoknot-stalled complex, the translocase EF-2 is seen to compress a hybrid-state tRNA into a strained conformation. We propose that this strain energy helps overcome the kinetic barrier to translocation and drives tRNA into the P-site, with EF-2 biasing this relaxation in one direction. The tRNA can thus be considered a molecular spring and EF-2 a Brownian ratchet in a spring-and-ratchet system within the translocation process.
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