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Regulation of Tyrosine Biosynthesis in Escherichia coli K-12: Isolation and Characterization of Operator Mutants

^a School of Microbiology, University of Melbourne, Parkville, Victoria, Australia

ABSTRACT

Mutant strains of Escherichia coli have been isolated in which the synthesis of two of the enzymes involved in tyrosine biosynthesis, 3-deoxy-D-arabinoheptulosonic acid-7 phosphate synthetase (tyr) and chorismate mutase T-prephenate dehydrogenase, is partially constitutive. The mutations involved are closely linked to aroF and tyrA, the structural genes of these enzymes. The gene in which the mutations occur has been designated aroK, and the gene sequence is aroK, aroF, tyrA. In aroK⁺/aroK diploids, the aroK allele only affects the structural genes in the cis position. The mutant allele aroK is not recessive to aroK⁺ and aroK/aroK⁺ strains exhibit the aroK phenotype of resistance to 4-aminophenylalanine. It is proposed that aroK is an operator locus for an aroF tyrA operon.

¹ Present address: Medical Biological Laboratory of the National Defence Research Organization TNO, Rijswijk (ZH), The Netherlands.

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