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- W1965822177 abstract "Abstract During the first 20 min of a nutritional shift-up in Escherichia coli the ratio of ribosomal protein to soluble protein synthesis is increased to a level four times that characteristic of balanced growth. To determine whether this exaggerated synthesis of ribosomal protein imposed any restrictions on the formation of soluble protein the induced synthesis of β-galactosidase was measured. Continuous synthesis of the enzyme was observed in the presence of 10 mM cyclic AMP which overcame the catabolite repression encountered in the shift-up medium. Studies on the influence of cyclic AMP upon the synthesis of ribosomal and total soluble protein revealed the cyclic nucleotides had no effect upon ribosomal protein synthesis while producing a marginal increase in the soluble protein formation. These investigations suggest that the exaggerated production of ribosomal protein during a shift-up does not restrict the synthesis of soluble protein. Induction of β-galactosidase during a shift-up at suboptimal concentrations of cyclic AMP (5 mM) resulted in a discontinuous pattern of enzyme synthesis in a wild-type strain of E. coli. Studies with a phosphodiesterase-less mutant indicated that in the presence of 5 mM cyclic AMP the synthesis of β-galactosidase was continuous. The addition of theophylline, an inhibitor of phosphodiesterase, to cells possessing an active phosphodiesterase increased the yield of β-galactosidase at 5 mM cyclic AMP. These studies indicate that during a nutritional shift-up, when transient catabolite repression is effective, the activity of phosphodiesterase is implicated in regulating the synthesis of β-galactosidase." @default.
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- W1965822177 date "1972-12-01" @default.
- W1965822177 modified "2023-09-27" @default.
- W1965822177 title "Ribosomal and soluble protein synthesis during a nutritional shift-up. Influence of cyclic AMP on β-galactosidase activity" @default.
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- W1965822177 doi "https://doi.org/10.1016/0005-2787(72)90381-4" @default.
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