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. 1971 Feb;68(2):367–371. doi: 10.1073/pnas.68.2.367

Regulation of Methionine Biosynthesis in Escherichia coli: Mapping of the metJ Locus and Properties of a metJ+/metJ- Diploid

Ching-Hsiang Su 1,2, Ronald C Greene 1,2
PMCID: PMC388939  PMID: 5277087

Abstract

MetJ- mutants of Escherichia coli have elevated nonrepressible levels of the enzymes of methionine biosynthesis and S-adenosylmethionine synthetase (ATP:L-methionine S-adenosyltransferase, EC 2.5.1.6). In E. coli, as in Salmonella typhimurium, the metJ locus is close to metB (95% cotransduction of metB and metJ markers), but in E. coli the order is reversed, with metJ mapping clockwise to metB. A stable merodiploid, heterozygous for metJ, is subject to repression by methionine. Thus, metJ functions via a diffusible product. MetJ could either be a regulatory locus or could code for an enzyme required for the synthesis of a methionine metabolite that functions in the control system.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ayling P. D., Chater K. F. The sequence of four structural and two regulatory methionine genes in the Salmonella typhimurium linkage map. Genet Res. 1968 Dec;12(3):341–354. doi: 10.1017/s0016672300011927. [DOI] [PubMed] [Google Scholar]
  2. Berg C. M., Curtiss R., 3rd Transposition derivatives of an Hfr strain of Escherichia coli K-12. Genetics. 1967 Jul;56(3):503–525. doi: 10.1093/genetics/56.3.503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. COHEN G., JACOB F. Sur la répression de la synthèse des enzymes intervenant dans la formation du tryptophane chez Escherichia coll. C R Hebd Seances Acad Sci. 1959 Jun 15;248(24):3490–3492. [PubMed] [Google Scholar]
  4. DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. FLAVIN M. Microbial transsulfuration: the mechanism of an enzymatic disulfide elimination reaction. J Biol Chem. 1962 Mar;237:768–777. [PubMed] [Google Scholar]
  6. Flavin M., Slaughter C. Synthesis of the succinic ester of homoserine, a new intermediate in the bacterial biosynthesis of methionine. Biochemistry. 1965 Jul;4(7):1370–1375. doi: 10.1021/bi00883a022. [DOI] [PubMed] [Google Scholar]
  7. GLANSDORFF N. TOPOGRAPHY OF COTRANSDUCIBLE ARGININE MUTATIONS IN ESCHERICHIA COLI K-12. Genetics. 1965 Feb;51:167–179. doi: 10.1093/genetics/51.2.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Greene R. C., Su C. H., Holloway C. T. S-Adenosylmethionine synthetase deficient mutants of Escherichia coli K-12 with impaired control of methionine biosynthesis. Biochem Biophys Res Commun. 1970 Mar 27;38(6):1120–1126. doi: 10.1016/0006-291x(70)90355-4. [DOI] [PubMed] [Google Scholar]
  9. Holloway C. T., Greene R. C., Su C. H. Regulation of S-adenosylmethionine synthetase in Escherichia coli. J Bacteriol. 1970 Nov;104(2):734–747. doi: 10.1128/jb.104.2.734-747.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ikeda H., Tomizawa J. I. Transducing fragments in generalized transduction by phage P1. I. Molecular origin of the fragments. J Mol Biol. 1965 Nov;14(1):85–109. doi: 10.1016/s0022-2836(65)80232-7. [DOI] [PubMed] [Google Scholar]
  11. Kaplan M. M., Flavin M. Cystathionine gamma-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis. J Biol Chem. 1966 Oct 10;241(19):4463–4471. [PubMed] [Google Scholar]
  12. Lawrence D. A., Smith D. A., Rowbury R. J. Regulation of methionine synthesis in Salmonella typhimurium: mutants resistant to inhibition by analogues of methionine. Genetics. 1968 Apr;58(4):473–492. doi: 10.1093/genetics/58.4.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Patte J. C., Le Bras G., Cohen G. N. Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K 12. Biochim Biophys Acta. 1967 Mar 22;136(2):245–247. doi: 10.1016/0304-4165(67)90069-4. [DOI] [PubMed] [Google Scholar]
  14. Rowbury R. J. Resistance to norleucine and control of methionine synthesis in Escherichia coli. Nature. 1965 May 29;206(987):962–963. doi: 10.1038/206962a0. [DOI] [PubMed] [Google Scholar]

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