Abstract
Amino-acid starvation in polyamine-auxotrophic bacteria grown in the presence of putrescine provokes a marked inhibition of protein synthesis. This inhibition is almost completely relieved in polyamine-depleted cells. The differential behaviour of bacterial protein synthesis depending on the endogenous levels of polyamines is not due to a change in the uptake of amino acids used to measure protein synthesis, nor to the decreased growth rate of polyamine-depleted cells. During leucine starvation, cells grown with putrescine synthesized a somewhat lower amount of high-molecular-weight proteins than polyamine-depleted bacteria. In addition, cells with normal endogenous levels of polyamines accumulated significant amounts of 62 and 41 kDa polypeptides as well as several low-molecular-weight peptides.
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