Regulation of guaC expression in Escherichia coli.
The guaC gene encodes GMP reductase, which converts GMP to inosine monophosphate. Regulation of guaC expression was examined by use of guaC-lac fusions created by Mu d1(lac). In these strains, beta-galactosidase is induced by guanine derivatives, and this induction is prevented by adenine. Our previous implication that glutamine acts as a negative effector of transcription was confirmed by showing that glutamine analogs (diazo-oxo-norleucine and methionine sulfoximine) can also induce beta-galactosidase. GMP was implicated as a likely candidate for the in vivo inducer by introducing a gpt block to prevent the conversion of guanine to GMP and a deoD block to prevent the interconversion of guanine and guanosine. Regulatory mutants were isolated by growth on lactose plus adenine. Though these showed high constitutive levels of beta-galactosidase, they were normal for the regulation of GMP reductase when the fusion was corrected by transduction to guaC+ or when guaC+ was introduced by plasmid complementation. The regulatory mutants were linked to guaC.
D004926:Escherichia coli / Q000235:genetics*; D050899:GMP Reductase; D005786:Gene Expression Regulation; D005973:Glutamine / Q000031:analogs & derivatives / Q000494:pharmacology; D006157:Guanosine Monophosphate / Q000378:metabolism; D007291:Inosine Monophosphate / Q000378:metabolism; D009154:Mutation; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics*; D011687:Purines / Q000494:pharmacology; D001616:beta-Galactosidase / Q000235:genetics
D011687:Purines; D005973:Glutamine; D007291:Inosine Monophosphate; D006157:Guanosine Monophosphate; D009247:NADH, NADPH Oxidoreductases; D050899:GMP Reductase; D001616:beta-Galactosidase