Summary
The metabolic fate of translation initiation factor after inhibition of protein synthesis by different means has been investigated. We have found a decay in initiation factor activity when protein synthesis is blocked by chloramphenicol but not during arginine starvation of PA1 (Rel−) or PA2 (Rel+) strains or during puromycin incubation. These results suggest that inactivation of certain initiation factors occurs when the regeneration of ribosomal subunits from polysomes is inhibited in the cells.
Complementation experiments indicate that IF3 factor activity is preferentially affected during chloramphenicol treatment.
Same preferential inhibition of IF3 activity seems to occur during “in vitro” incubation of crude IF. 70S ribosomes or 30S subunits protect this factor against the inactivation. Preliminary results seem tosuggest that ATP is implicated in this “in vitro” inactivation process.
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Communicated by H. G. Wittmann
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Legault-Demare, L., Jeantet, C. & Gros, F. Metabolic fate of initiation factors after inhibition of protein synthesis in Escherichia coli . Molec. Gen. Genet. 125, 301–318 (1973). https://doi.org/10.1007/BF00276586
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DOI: https://doi.org/10.1007/BF00276586