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S-adenosyl methionine requiring mutants in Saccharomyces cerevisiae: Evidences for the existence of two methionine adenosyl transferases

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Summary

Mutants requiring S-adenosyl methionine (SAM) for growth have been selected in Saccharomyces cerevisiae. Two classes of mutants have been found. One class corresponds to the simultaneous occurrence of mutations at two unlinked loci SAM1 and SAM2 and presents a strict SAM requirement for growth on any medium. The second class corresponds to special single mutations in the gene SAM2 which lead to a residual growth on minimal medium but to normal growth on SAM supplemented medium or on a complex medium like YPGA not containing any SAM. These genetic data can be taken as an indication that Saccharomyces cerevisiae possesses two isoenzymatic methionine adenosyl transferases (MAT). In addition, SAM1 and SAM2 loci have been identified respectively with the ETH-10 and ETH2 loci previously described.

Biochemical evidences corroborate the genetic results. Two MAT activities can be dissociated in a wild type extract (MATI and MATII) by DEAE cellulose chromatography. Mutations at the SAM1 locus lead to the absence or to the modification of MATII whereas mutations at the SAM2 locus lead to the absence or to the modification of MATI. Moreover, some of our results seem to show that MATI and MATII are associated in vivo.

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References

  • Ahmed, A.: Mechanism of repression of methionine biosynthesis in Escherichia coli. Molec. gen. Genet. 123, 299–324 (1973)

    Google Scholar 

  • Anderson, W.B., Horne, R.N., Nordlie, R.C.: Glucose dehydrogenase activity of yeast glucose-6-phosphate dehydrogenase. II. Kinetic studies of the mode of activation by bicarbonate, phosphate and sulfate. Biochemistry 7, 3974–4004 (1968)

    Google Scholar 

  • Antoniewski, J., de Robichon-Szulmajster, H.: Biosynthesis of methionine and its control in wild type and regulatory mutants of Saccharomyces cerevisiae. Biochimie 55, 529–539 (1973)

    Google Scholar 

  • Burgess, R.R.: A new method for the large scale purification of Escherichia coli deoxyribonucleic acid-dependent ribonucleic acid polymerase. J. biol. Chem. 244, 6160–6167 (1969)

    Google Scholar 

  • Cherest, H., Eichler, F., de Robichon-Szulmajster, H.: Genetic and regulatory aspects of methionine biosynthesis in Saccharomyces cerevisiae. J. Bact. 97, 328–336 (1969)

    Google Scholar 

  • Cherest, H., Surdin-Kerjan, Y., Antoniewski, J., de Robichon-Szulmajster, H.: S-adenosyl methionine-mediated repression of methionine biosynthetic enzymes in Saccharomyces cerevisiae. J. Bact. 114, 928–933 (1973a)

    Google Scholar 

  • Cherest, H., Surdin-Kerjan, Y., Antoniewski, J., de Robichon-Szulmajster, H.: Effects of regulatory mutations upon methionine biosynthesis in Saccharomyces cerevisiae; loci eth2-eth3-eth10. J. Bact. 115, 1084–1093 (1973b)

    Google Scholar 

  • Chiang, P.K., Cantoni, G.L.: Activation of methionine for transmethylation. Purification of the S-adenosyl méthionine synthetase of Baker's yeast and its separation into two forms. J. biol. Chem. 252, 4506–4513 (1977)

    Google Scholar 

  • Chou, T.C., Lombardini, J.B.: A rapid assay procedure for ATP: L-methionine adenosyl transferase. Biochim. biophys. Acta (Amst.) 276, 399–409 (1972)

    Google Scholar 

  • Chou, T.C., Talalay, P.: The mechanism of S-adenosyl-L-methionine synthesis by purified preparations of Baker's yeast. Biochemistry 11, 1065–1073 (1972)

    Google Scholar 

  • Ferro, A.J., Spence, D.K.: Induction and repression of S-adenosyl methionine and methionine biosynthetic systems of Saccharomyces cerevisiae. J. Bact. 116, 812–817 (1973)

    Google Scholar 

  • Fesneau, C., de Robichon-Szulmajster, H., Fradin, A., Feldman, H.: tRNAs undermethylation in a met-regulatory mutant of Saccharomyces cerevisiae. Biochimie 57, 49–59 (1975)

    Google Scholar 

  • Galzy, P., Slonimski, P.P.: Evolution de la constitution enzymatique de la levure cultivée sur acide lactique ou sur glucose comme seule source de carbone. C.R. Acad. Sci. (Paris) 245, 2556–2558 (1957)

    Google Scholar 

  • Gornall, A.G., Bardawill, C.J., David, M.M.: Determination of serum proteins by means of the biuret reaction. J. biol. Chem. 177, 715–766 (1949)

    Google Scholar 

  • Greene, R.C.: Kinetic studies of the mechanism of S-adenosylmethionine synthetase from yeast. Biochemistry 8, 2255–2265 (1969)

    Google Scholar 

  • Greene, R.C., Nunter, J.S.V., Coch, E.H.: Properties of metK mutants of Escherichia coli K12. J. Bact. 115, 57–67 (1973)

    Google Scholar 

  • Greene, R.C., Hunter, J.S.V., Coch, E.H.: Genetic characterization of the METK locus in Escherichia coli K12. J. Bact. 122, 1144–1152 (1975)

    Google Scholar 

  • Hafner, E.W., Tabor, C.W., Tabor, H.: Isolation of a metK mutant with a temperature sensitive S-adenosyl methionine synthetase. J. Bact. 132, 832–840 (1977)

    Google Scholar 

  • Hobson, A.: The synthesis of S-adenosyl methionine by mutants with defects in S-adenosyl methionine synthetase. Molec. gen. Genet. 144, 87–95 (1976)

    Google Scholar 

  • Hobson, A.C., Smith, D.A.: S-Adenosylmethionine synthetase in methionine regulatory mutants of Salmonella typhimurium. Molec. gen. Genet. 126, 7–18 (1973)

    Google Scholar 

  • Johnston, J.R., Mortimer, R.K.: Use of snail digestive juice in isolation of yeast spore tetrads. J. Bact. 78, 292 (1959)

    Google Scholar 

  • Knudsen, R.C., Moore, K., Yall, I.: Uptake and utilization of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine in an adenine mutant of Saccharomyces cerevisiae. J. Bact. 98, 629–636 (1969)

    Google Scholar 

  • Lombardini, J.B., Coulter, A.W., Talalay, P.: Analogues of methionine as substrates and inhibitors of the methionine adenosyltransferase reaction. Molec. Pharmacol. 6, 481–499 (1970)

    Google Scholar 

  • McClary, D.O., Nulty, W.T., Miller, G.R.: Effect of potassium versus sodium in the sporulation of Saccharomyces cerevisiae. J. Bact. 78, 362–368 (1959)

    Google Scholar 

  • Martin, R.G., Ames, B.N.: A method for determining the sedimentation behavior of enzymes: Application to protein mixtures. J. biol. 236, 1372–1379 (1961)

    Google Scholar 

  • Masselot, M., de Robichon-Szulmajster, H.: Nonsense mutation in the regulatory gene ETH2 involved in methionine biosynthesis in Saccharomyces cerevisiae. Genetics 71, 535–550 (1972)

    Google Scholar 

  • Masselot, M., de Robichon-Szulmajster, H.: Methionine biosynthesis in Saccharomyces cerevisiae: Mutations at the regulatory locus ETH2. I. Genetic data. Molec. gen. Genet. 129, 339–348 (1974a)

    Google Scholar 

  • Masselot, M., de Robichon-Szulmajster, H.: Methionine biosynthesis in Saccharomyces cerevisiae: Mutations at the regulatory locus ETH2. II. Physiological and biochemical data. Molec. gen. Genet. 129, 349–362 (1964b)

    Google Scholar 

  • Masselot, M., de Robichon-Szulmajster, H.: Methionine biosynthesis in Saccharomyces cerevisiae: Mutations at the regulatory locus ETH2. III. Study of several homoallelic and heteroallelic diploids. Molec. gen. Genet. 129, 362–368 (1974c)

    Google Scholar 

  • Mudd, S.H.: Activation of methionine for transmethylation. VI. Enzyme bound tripolyphosphate as an intermediate in the reaction catalyzed by the methionine activating enzyme of Baker's yeast. J. biol. Chem. 238, 2156–2163 (1963)

    Google Scholar 

  • Mudd, S.H., Cantoni, G.L.: Activation of methionine for transmethylation. III. The methionine-activating enzyme of Baker's yeast. J. biol. Chem. 231, 481–492 (1958)

    Google Scholar 

  • Murphy, J.F., Spence, K.D.: Transport of S-adenosyl-methionine in Saccharomyces cerevisiae. J. Bact. 111, 778–783 (1972)

    Google Scholar 

  • Nagai, S., Flavin, M.: Synthesis of acetylhomoserine. In: Methods in enzymology, Vol. XVII B, pp. 423–424 (Tabor, H. and Tabor, C.W., eds.) New York: Academic Press 1971

    Google Scholar 

  • Nehrlich, S.C., Shapiro, S.K., cited by S.K. Shapiro and A.J. Ferro. Metabolism of adenosyl methionine during life cycle of Enterobacter aerogenes and Saccharomyces cerevisiae. In: The biochemistry of adenosyl methionine, pp. 58–76 (F. Salvatore, E. Borek, V. Zappia, H.G. Williams-Ashman, F. Schlenk, eds.) New York: Columbia University Press 1977

    Google Scholar 

  • Orr, C.W.M.: The inhibition of catalase (hydrogen-peroxide: hydrogen peroxide oxidoreductase EC 1.11.1.6) by ascorbate. In: Methods in enzymology, Vol. XVIIIA, pp. 59–62 (McCormick, D.B. and Wright, L.D., eds.) New York: Academic Press 1970

    Google Scholar 

  • Racker, E.: Alcohol dehydrogenase from Baker's yeast. In: Methods in enzymology I, pp. 500–503 (Colowick, S.P. and Kaplan, N.O., eds.). New York: Academic Press 1955

    Google Scholar 

  • Smith, M.M.: Molecular weights of proteins and some other materials including sedimentation, diffusion and frictional coefficients and partial specific volumes. In: Handbook of biochemistry. Selected data for molecular biology C1-C35 (Sober, H.A. and Harte, R.A., eds.). Cleveland, Ohio: The Chemical Rubber Co. Publisher 1968

    Google Scholar 

  • Snow, R.: An enrichment method for auxotrophic yeast mutants using the antibiotic nystatin. Nature (Lond.) 211 206–207 (1966)

    Google Scholar 

  • Surdin, Y.: La semi-aldéhyde aspartique deshydrogénase chez Saccharomyces cerevisiae: propriétés et régulation. Europ. J. Biochem. 2, 341–348 (1967)

    Google Scholar 

  • Stauffer, G.V., Brenchley, J.E.: Influence of methionine biosynthesis on serine transhydroxymethylase regulation in Salmonella typhimurium LT2. J. Bact. 129, 740–749 (1977)

    Google Scholar 

  • Torriani, A.: Alkaline phosphatase of E. coli. In: Methods in enzymology, Vol. XIIB, pp. 212–218 (Grossman, L. and Moldave, K., eds.). New York: Academic Press 1968

    Google Scholar 

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Authors and Affiliations

  1. Laboratoire d'Enzymologie du C.N.R.S., F-91190, GIF-sur-Yvette, France

    Hélène Cherest & Yolande Surdin-Kerjan

  2. Laboratoire de Génétique Physiologique, IBMC du C.N.R.S., 15, rue Descartes, F-67000, Strasbourg, France

    Françoise Exinger & François Lacroute

Authors
  1. Hélène Cherest
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  2. Yolande Surdin-Kerjan
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  3. Françoise Exinger
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  4. François Lacroute
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Communicated by W. Gajewski

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Cherest, H., Surdin-Kerjan, Y., Exinger, F. et al. S-adenosyl methionine requiring mutants in Saccharomyces cerevisiae: Evidences for the existence of two methionine adenosyl transferases. Molec. Gen. Genet. 163, 153–167 (1978). https://doi.org/10.1007/BF00267406

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  • DOI: https://doi.org/10.1007/BF00267406

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