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. 1967 Jan;93(1):254–263. doi: 10.1128/jb.93.1.254-263.1967

Inducible System for the Utilization of β-Glucosides in Escherichia coli I. Active Transport and Utilization of β-Glucosides1

S Schaefler a,2
PMCID: PMC314996  PMID: 5335892

Abstract

Wild-type Escherichia coli strains (β-gl−) do not split β-glucosides, but inducible mutants (β-gl+) can be isolated which do so. This inducible system consists of a β-glucoside permease and an aryl β-glucoside splitting enzyme. Both can be induced by aryl and alkyl β-glucosides. In β-gl− and noninduced β-gl+ cells, C14-labeled thioethyl β-glucoside (TEG) is taken up by a constitutive permease, apparently identical with a glucose permease (GP). This permease has a high affinity for α-methyl glucoside and a low affinity for aryl β-glucosides. No accumulation of TEG occurs in a β-gl− strain lacking glucose permease (GP−). In induced β-gl+ strains, there appears a second β-glucoside permease with low affinity for α-methyl glucoside and high affinity for aryl β-glucosides. Autoradiography shows that TEG is accumulated by the β-glucoside permease and glucose permease in two different forms (one being identical with TEG, the other probably phosphorylated TEG). In GP+ β-gl+ strains with high GP activity, alkyl β-glucosides induce the enzyme and the β-glucoside permease after a prolonged induction lag, and they competitively inhibit the induction by aryl β-glucosides. The induction lag and competition do not exist in GP− β-gl+ strains. It is assumed that phosphorylated alkyl and thioalkyl β-glucosides inhibit the induction, and that this inhibition is responsible for the induction lag.

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Selected References

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