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Upon transpeptidylation, the 3′ end of aminoacyl-tRNA (aa-tRNA) in the ribosomal A site enters the A/P hybrid state. We report that transpeptidylation of Phe-tRNA to fMetPhe-tRNA on Escherichia coli ribosomes substantially lowers the kinetic stability of the ribosome–tRNA complex and decreases the affinity by 18.9 kJ mol−1. At the same time, the free energy of activation of elongation factor G dependent translocation decreases by 12.5 kJ mol−1, indicating that part of the free energy of transpeptidylation is used to drive translocation kinetically. Thus, the formation of the A/P hybrid state constitutes an important element of the translocation mechanism. |
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