Abstract

l-Arabinose is transported into Escherichia coli via two independent transport systems, a system possessing relatively low affinity for arabinose, the araE system, and a system of higher affinity for arabinose, the araFG system. In the work reported here we demonstrate that insertion of the Mu- lac bacteriophage isolated by Casadaban & Cohen (1979) permits a reliable measurement of the expression of these two operons. Using appropriate Mu- lac insertion strains we found that both of the arabinose transport operons can be induced approximately 150-fold by the presence of arabinose, and that induction of both transport operons requires CRP (cyclic AMP receptor protein), but that their catabolite sensitivities differ from one another. In addition, we show that the araC + allele is dominant to the C c allele in the control of the transport operons, just as is found in the araBAD operon.

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