Watson et al
            14-33

In vivo Peptide Bond formation & growth of the polypeptide chain


    The amino acids in the ribosome are attached to their respective tRNAs by an ester bond (R - O - R) between the carboxyl terminus and the amino acceptor stem (left). During formation of a peptide bond, the ester bond of the amino acid in the (P)eptidyl site is cleaved, and Peptidyl Transferase catalyzes a reaction (see Note) between its carboxyl terminus and the amino terminus of the amino acid in the (A)mino site. This transfers the P-site amino acid to the A-site amino acid, and the original amino terminus remains unmodifiedThe polypeptide thus "grows" from the amino terminus to the carboxyl terminus.

    Note: In vitro formation of the peptide bond is often described as a dehydration reaction that involves the splitting out of an
H20. However, the in vivo reaction does not.

    Note first that the
C terminus of the amino acid in the P site participates in the ester bond as a carbonyl radical (-C=O), without a separate -OH group. The peptide bond is formed by a nucleophilic attack of the N of the A site amino terminus on this carbonyl C. The -O- of the ester bond remains attached to the 3'-C of the tRNA. The proton on the 2'-C then shifts to the 3'-C to restore the -OH terminus of the uncharged tRNA, and a proton from the amino terminus of the incoming amino acid the shifts to the 2'-C. The in vivo reaction balances, without production of an H20 molecule.


Figure after ©2008 by Watson et al.; All text material ©2012  by Steven M. Carr