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Mutations affectant le catabolisme du glucuronate chez Escherichia coli K12

Studies of mutations in glucuronate catabolism in Escherichia coli K12

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Summary

In a study of the regulation of the hexuronate system in Escherichia coli K 12, two classes of glucuronate negative mutants were isolated and characterized.

The first class was composed of eight mutants specifically deficient for the enzyme mannonic oxidoreductase. Glucuronate via fructuronate could still induce the other four hexuronate system enzymes in these strains although it was no more metabolized; galacturonate is normally used.

The corresponding mutations in the uxu B locus were localized on the chromosome of E. coli by interrupted and non-interrupted conjugations. They all mapped at 86 min close to the uxu A locus, the structural gene of mannonic hydrolase which is the following functional enzyme in glucuronate catabolism.

Biochemical characterizations of uxu B mutants using thermal inactivation and pCMB inhibition of residual mannonic oxidoreductase activity, as well as dominance studies with diploid strains strongly suggested that the uxu B locus was the structural gene of mannonic oxidoreductase.

The second class of mutations involved pleiotropic deficiency in both mannonic oxidoreductase and hydrolyase. Their genetic mapping and the preliminary fine structure analysis of the uxu region showed they were deletions extending into uxu A and uxu B genes. These properties agreed very well with independent physiological results (Robert-Baudouy, Portalier et Stoeber, 1973) and was in agreement with the existence of an unique operon at least composed of uxu A and uxu B structural genes.

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Bibliographie

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Robert-Baudouy, J.M., Portalier, R.C. Mutations affectant le catabolisme du glucuronate chez Escherichia coli K12. Molec. Gen. Genet. 131, 31–46 (1974). https://doi.org/10.1007/BF00269385

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