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Published June 2013 | public
Journal Article

Structural Basis of the Translational Elongation Cycle

Abstract

The sequential addition of amino acids to a growing polypeptide chain is carried out by the ribosome in a complicated multistep process called the elongation cycle. It involves accurate selection of each aminoacyl tRNA as dictated by the mRNA codon, catalysis of peptide bond formation, and movement of the tRNAs and mRNA through the ribosome. The process requires the GTPase factors elongation factor Tu (EF-Tu) and EF-G. Not surprisingly, large conformational changes in both the ribosome and its tRNA substrates occur throughout protein elongation. Major advances in our understanding of the elongation cycle have been made in the past few years as a result of high-resolution crystal structures that capture various states of the process, as well as biochemical and computational studies.

Additional Information

© 2013 Annual Reviews. This paper was authored by employees of the British Government as part of their official duties and is therefore subject to Crown Copyright. Reproduced with the permission of the Controller of Her Majesty's Stationery Office/Queen's Printer for Scotland and the UK Medical Research Council. We thank T. Martin Schmeing for providing us Figure 1 and panels derived from it and several members of the ribosome community and the reviewers for their critical feedback. This work was supported by Medical Research Council (UK) grant U105184332, the Wellcome Trust, the Agouron Institute and the Louis-Jeantet Foundation (V.R.) and a Research Fellowship from Peterhouse, Cambridge (R.M.V.). The authors are not aware of any affiliations, memberships, funding, or financial holdings that might be perceived as affecting the objectivity of this review.

Additional details

Created:
August 19, 2023
Modified:
October 18, 2023