Peptidyl transferase activity in rat skeletal muscle ribosomes after protein restriction.

Rats were fed for 6 consecutive days a diet containing casein supplemented with 3 g/kg methionine. The protein level was either 20% or 3%. Skeletal muscle ribosomes were isolated and the activity of the ribosomal enzyme peptidyl transferase was determined. [3H]puromycin acted as acceptor for tRNA bound peptide provided it was located at the ribosomal peptidyl site. The results showed that the rate of peptidyl transferase activity was 13% lower after protein restriction. The differences amounted to 6% when diphtheria toxin and NAD were added as an inhibitor of elongation factor2. This factor catalyzes translocation of peptidyl-tRNA from ribosomal acceptor to peptidyl site. Between 0.11 and 0.15 pmoles peptidyl-tRNA per pmole ribosome were originally accessable as a substrate for peptidyl transferase. The results indicate that peptidyl transferase contributes to a decrease in protein synthesis after protein restriction; but that other components also contribute to the decrease observed.