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S-adenosylmethionine synthetase in methionine regulatory mutants of Salmonella typhimurium

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Summary

In wild-type bacteria, S-adenosylmethionine (SAM) synthetase activity was repressed by growth in methionine. MetJ regulatory mutants had elevated activities which did not show this repression. Two metK mutants with normal regulation of the methionine biosynthetic enzymes had elevated Km's (methionine) for SAM synthetase while five metK mutants with constitutive methionine enzymes showed no measurable SAM synthetase activity. One mutant, metK X721, similar in phenotype to these five had a wild-type level of SAM synthetase in conditions where SAM decarboxylase activity was blocked. By using an F′-factor carrying the metK region of the genome, this mutant was shown to complement six other metK mutants.

These results indicate that SAM or a derivative of it, rather than methionine itself, is the co-repressor of the methionine system, regulatory abnormalities resulting from the absence or reduction of the amount of SAM formed by the SAM synthetase reaction. As SAM is essential for bacteria it is likely that there is some alternative biosynthetic route for SAM.

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References

  • Cantoni, G. L.: S-adenosylmethionine-revisted. In: Transmethylation and methionine biosynthesis. (Shapiro, S. K., Schlenk, F., eds.), p. 21–32. Chicago, Illinois: Chicago Univ. Press 1965

    Google Scholar 

  • Chater K. F.: Dominance of the wild-type alleles of methionine regulatory genes in Salmonella typhimurium. J. gen. Microbiol. 70 95–109 (1970)

    Google Scholar 

  • Childs, J. D., Smith, D. A.: New methionine structural gene in Salmonella typhimurium. J. Bact. 100, 377–382 (1969)

    Google Scholar 

  • Duerre, S. A., Schlenk, F.: Formation and metabolism of S-adenosylhomocysteine in yeast. Arch. Biochem. Biophys. 96, 575–579 (1962)

    Google Scholar 

  • Greene R. C., Su, C.-H., Holloway, C. T.: S-adenosylmethionine synthetase deficient mutants of Escherichia coli K12 with impaired control of methionine biosynthesis. Biochem. biophys. Res. Commun. 38, 1120–1126 (1970)

    Google Scholar 

  • Gross, T. S.: Biochemical aspects of the regulation of methionine biosynthesis in Salmonella typhimurium. Ph. D. thesis, University College, University of London (1969)

  • Gross, T. S., Rowbury, R. J.: Biochemical and physiological properties of methionyl-sRNA synthetase mutants of Salmonella typhimurium. J. gen. Microbiol. 65, 5–21 (1971)

    Google Scholar 

  • Holloway, D. A., Greene, R. C., Su, C.-H.: Regulation of S-adenosylmethionine synthetase in Escherichia coli. J. Bact. 104, 734–747 (1970)

    Google Scholar 

  • 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 58, 473–492 (1968)

    Google Scholar 

  • Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein estimation with the Folin and Ciocalteau reagent. In: Methods in enzymology (Colowick, D. S., and Kaplan, N. O., eds.) vol. III, p. 448–450. New York: Academic Press 1957

    Google Scholar 

  • Mass, W. K., Leifer, Z., Poindexter, J.: Studies with mutants blocked in the synthesis of polyamines. Ann. N. Y. Acad. Sci. 171, 957–967 (1970)

    Google Scholar 

  • Minson, A. C., Smith, D. A.: Methionine regulatory defects in Salmonella typhimurium arising from amber-suppressible mutations. J. gen. Microbiol. 70, 471–476 (1972)

    Google Scholar 

  • Mudd, S. H., Finkelstein, J. D., Irrevere, F., Laster, L.: Transsulfuration in mammals. J. biol. Chem. 240, 4382–4392 (1965)

    Google Scholar 

  • Savin, M. A., Flavin, M., Slaughter, C.: Regulation of homocysteine biosynthesis in Salmonella typhimurium. J. Bact. 111, 547–556 (1972)

    Google Scholar 

  • Shapiro, S. K., Mather, A. N.: The enzymatic decomposition of S-adenosyl-l-methionine. J. biol. Chem. 233, 631–633 (1958)

    Google Scholar 

  • Smith, D. A.: Some aspects of the genetics of methionineless mutants of Salmonella typhimurium. J. gen. Microbiol. 24, 335–353 (1961)

    Google Scholar 

  • Smith, D. A.: S-amino acid metabolism and its regulation in Escherichia coli and Salmonella typhimurium. Advanc. Genet. 16, 141–165 (1971)

    Google Scholar 

  • Smith, D. A., Childs, J. D.: Methionine genes and enzymes of Salmonella typhimurium. Heredity 21, 265–286 (1966)

    Google Scholar 

  • Smith, H. O., Levine, M.: A phage P22 gene controlling integration of prophage. Virology 31, 207–216 (1967)

    Google Scholar 

  • Tabor, H., Rosenthal, S. M., Tabor, C. W.: The biosynthesis of spermidine and spermine from putrescine and methionine. J. biol. Chem. 233, 907–914 (1958)

    Google Scholar 

  • Tabor, H., Tabor, C. W.: Enzymatic synthesis of radioactive S-adenosyl-l-methionine. In: Methods in enzymology (Colnwick, D. S., and Kaplan, N. O., eds.), vol. XVII B, p. 393–397. New York: Academic Press 1971

    Google Scholar 

  • Whitehouse, J. M., Smith, D. A.: Methionine and vitamin B12 repression and precursor induction in the regulation of homocysteine methylation in Salmonella typhimurium. Molec. gen. Genet. 120, 341–353 (1973)

    Google Scholar 

  • Wickner, R. B., Tabor, C. W., Tabor, H.: Purification of adenosylmethionine decarboxylase from Escherichia coli: evidence for covalently bound pyruvate. J. biol. Chem. 245, 2132–2139 (1970)

    Google Scholar 

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Communicated by H. Böhme

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Hobson, A.C., Smith, D.A. S-adenosylmethionine synthetase in methionine regulatory mutants of Salmonella typhimurium . Molec. gen. Genet. 126, 7–18 (1973). https://doi.org/10.1007/BF00333477

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  • DOI: https://doi.org/10.1007/BF00333477

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