Abstract
During protein synthesis, the ribosome translates the genetic information carried by the mRNA into the amino acid sequence of proteins with the help of adaptor molecules, aminoacyl-tRNAs (aa-tRNA). In each round of elongation, the ribosome selects the correct (cognate) aa-tRNA corresponding to the mRNA codon from the total cellular pool of aa-tRNAs. The delivery of aa-tRNA to the decoding site (A site), where tRNA recognition and selection takes place, is brought about by elongation factor Tu (EF-Tu). The recognition of aa-tRNA by the ribosome occurs via a series of selection steps that control the stepwise movement of aa-tRNA from EF-Tu into the A site and the accommodation of the aminoacyl end of the aa-tRNA in the peptidyl transferase center. Accommodation is followed by peptide bond formation between the A-site aa-tRNA and peptidyl-tRNA in the P site that results in the elongation of the nascent peptide chain by one amino acid. The functional centers of the ribosomes are composed mostly of rRNA. Thus, understanding decoding and peptide bond formation requires answers to several fundamental questions: (i) how does the rRNA machinery recognize tRNAs and mRNAs? (ii) how does the ribosome discriminate between very similar cognate and near-cognate tRNAs which change identity in every round of elongation? (iii) how does the ribosome balance the requirements for speed and accuracy? and (iv) how does rRNA catalyze peptide bond formation? The goal of this review is to summarize the recent progress towards answering these questions.
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Rodnina, M.V. (2011). Mechanisms of decoding and peptide bond formation. In: Rodnina, M.V., Wintermeyer, W., Green, R. (eds) Ribosomes. Springer, Vienna. https://doi.org/10.1007/978-3-7091-0215-2_16
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