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Effect of methionine and vitamin B-12 on the activities of methionine biosynthetic enzymes in metJ mutants of Escherichia coli K12
Authors:R C Greene  R D Williams  H F Kung  C Spears  H Weissbach
Affiliation:1. Basic Science Laboratory, Veterans Administration Hospital and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27705 U.S.A.;2. Roche Institute of Molecular Biology, Nutley, New Jersey 07110 U.S.A.
Abstract:The effects of supplementation of growth medium with high concentrations of methionine (5 mm) and/or vitamin B12 (10 nm) on the activities of five enzymes of the methionine regulon were measured in wild-type Escherichia coli K12, a metJ prototrophic and three metJ methionine auxotrophic derivatives. Growth on vitamin B12 causes lowering of the activities of the non-B12 methyltransferase while growth on methionine causes elevation of its activity in all four metJ mutants. The previous observation that this enzyme is not repressed by vitamin B12 addition in metH mutants together with our observation that vitamin B12 causes repression in mutants (metF) unable to synthesize the donor for homocysteine methylation supports the model of Kung et al. (10) that the holo-B12-methyltransferase functions as a repressor of synthesis of the non-B12-methyltransferase. Growth on methionine causes lowering of cystathionase activity, and growth on vitamin B12 results in elevation of cystathionase activity in a metJ prototroph and one metJ auxotroph. The metJmetA strain (RG326) has a higher than normal level of cystathionase while the metJmetF strain (RG191) has lower than normal cystathionase activity. These results indicate the existence of a metJ independent system that modulates the activity of cystathionase possibly in response to changes in concentration of unidentified metabolite(s).
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