Abstract
At any given time in the course of polypeptide elongation, the ribosome is attached to the coding region of mRNA and retains the molecule of the peptidyl-tRNA (Fig. 9.1). The peptidyl-tRNA is a nascent peptide chain bound through its C-terminus to the tRNA that has donated the last amino acid residue to the peptide. Such a ribosome can bind or may become capable of binding the aminoacyl-tRNA determined by the next mRNA codon (Fig. 9.1 step I). The binding of the aminoacyl-tRNA results in the retained peptidyl-tRNA and the newly bound aminoacyl-tRNA being present on the ribosome simultaneously. Their side-by-side location and the catalytic activity of the ribosome are prerequisites of the transpeptidation reaction: the C-terminus of the peptidyl residue is transferred from the tRNA (to which it had previously been bound) to the amino group of the aminoacyl-tRNA (Fig. 9.1 step II). As a result, the formation of a new peptidyl-tRNA with the peptide elongated by one amino acid residue at the C-end takes place; the other product of the transpeptidation reaction is the deacylated tRNA. In order to make the ribosome competent to bind the next aminoacyl-tRNA, the intraribosomal ligands (tRNAs and mRNA) must be displaced, resulting in the vacation of a place for the aminoacyl-tRNA and in the positioning of the next mRNA codon (Fig. 9.1 step III); this step is called translocation.
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Spirin, A.S. (1999). Functional Activities and Functional Sites of the Ribosome. In: Ribosomes. Cellular Organelles. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7817-8_9
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DOI: https://doi.org/10.1007/978-1-4615-7817-8_9
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