The Formation of the Peptide Bond on Ribosomes
Polypeptide chains of proteins are synthesized on ribosomes by a cyclic reaction during which the nascent polypeptide is transferred from polypeptidyl-tRNA to the neighbouring aminoacyl-tRNA. In each completed cycle of the reaction the polypeptidyl-tRNA is extended by one aminoacid residue, tRNA which has lost the polypeptide is excluded from the ribosome and a new aminoacyl-tRNA elected by the codonanticodon interaction enters the reaction [1–3]. In addition to the ribosome and the two tRNA derivatives soluble enzymes from the postribosomal supernatant are involved in the cycle. The mutual relations between the ribosome and supernatant enzymes are clearly shown in the poly A directed cell free Escherichia coli system synthesizing lysine peptides [4, 5]. Figure 1 shows the course of the synthesis of lysine peptides attached to tRNA in the complete system. A series of intermediates of polylysine synthesis is formed ranging from dilysyl-tRNA up to octalysyl-tRNA [6, 7]. When supernatant enzymes are omitted from the medium only dilysyl-tRNA is formed with a minor trace of trilysyl-tRNA the amount of which depends on the procedure used for washing the ribosomes  (Fig. 2).
KeywordsTerminal Sequence Nascent Polypeptide Magnesium Acetate Nascent Peptide Aminoacid Residue
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