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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Interactions of the Escherichia coli methionine repressor with the metF operator and with its corepressor, S-adenosylmethionine.

The metJ gene encoding the methionine aporepressor was placed under the control of a strong and inducible promoter, ptac. Bacterial strains carrying the recombinant plasmid pIP35 overproduced the regulatory protein by a factor of 200 over the wild type strain as determined by the immunoblot technique. The purified metJ gene product negatively controls the expression of the metF gene, in a cell-free system as shown by repression of beta-galactosidase synthesis under the control of the metF promoter. The metJ protein binds to a DNA fragment containing the potential operator of the metF gene with an affinity which is 10 times greater in the presence of S-adenosylmethionine than in its absence. Equilibrium dialysis experiments showed that the met aporepressor binds 2 mol of S-adenosylmethionine per mol of dimer with a dissociation constant of 200 microM.[1]

References

  1. Interactions of the Escherichia coli methionine repressor with the metF operator and with its corepressor, S-adenosylmethionine. Saint-Girons, I., Belfaiza, J., Guillou, Y., Perrin, D., Guiso, N., Bârzu, O., Cohen, G.N. J. Biol. Chem. (1986) [Pubmed]
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