We have studied the parameters of
protein synthesis in a number of Escherichia coli strains after a shift-down from
glucose-minimal to
succinate-minimal medium. One group of strains, including K-12(lambda) (ATCC 10798) and NF162, showed a postshift translational yield of 50 to 65% and a 2- to 2.5-fold increase in the functional lifetime of general messenger
ribonucleic acid. There was no change in the lag time for
beta-galactosidase induction in these strains after the shift-down. A second group, including W1 and W2, showed no reduction in translational yield, no change in the functional lifetime of messenger
ribonucleic acid, and a 50% increase in the lag time for
beta-galactosidase induction. Evidence is presented which indicates that this increased lag time is not the result of a decreased rate of
polypeptide chain propagation. A third group of strains, including NF161, CP78, and NF859, showed an intermediate pattern: translational yield was reduced to about 75% of normal, and the messenger
ribonucleic acid functional lifetime was increased by about 50%. Calculation of the relative postshift rates of translational initiation gave about 0.2, 1.0, and 0.5, respectively, for the three groups. There was no apparent correlation between the ability to control translation and the genotypes of these strains at the relA, relX, or spoT loci. Measurements of the induction lag for
beta-galactosidase during short-term
glucose starvation or after a down-shift induced by
alpha-methylglucoside indicated that these regimens elicit responses that are physiologically distinct from those elicited by a
glucose-to-
succinate shift-down.