Abstract

Consistent with the previous work by Pestka ( Antimicrob. Agents Chemother. 5, 255, 1974) on the binding of erythromycin to polyribosomes, we found that erythromycin does not inhibit protein synthesis catalyzed by polyribosomes. This is due to the presence of nascent peptidyl tRNA on the naturally occurring polyribosomes. In a soluble extract from E. coli pretreated to remove the ribosome releasing factor, polyribosomes without nascent polypeptides remain intact and can catalyze protein synthesis in the absence of initiation. In this system erythromycin effectively inhibited protein synthesis. The inhibition by erythromycin was caused by premature release of oligopeptidyl tRNA from polyribosomes.

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