Abstract
Protein synthesis in a polyamine-auxotrophic mutant of E. coli cultivated in the absence and presence of putrescine has been studied. The ratio of in vivo polypeptide synthesis under both conditions was the same as that obtained with cell-free extracts derived from polyamine-depleted and supplemented bacteria. The markedly reduced activity in systems from polyamine starved cells is most probably due to a poorly efficient initiation step. The estimation of nascent peptide chains and their release from tRNA support the idea that polypeptide elongation and termination processes do not have decreased rates in systems from polyamine-depleted bacteria.
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