Archives of Microbiology

, Volume 101, Issue 1, pp 59–70 | Cite as

Linkage of the Salmonella typhimurium chromosomal loci encoding for the cytochrome-linked l-α-glycerophosphate dehydrogenase and amylomaltase activities

  • Efraín Aceves-Piña
  • Manuel V. Ortega
  • Mireya Artís
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Abstract

Mutant SM6, of Glp- Mal- phenotype, was isolated from Salmonella typhimurium LT2 after treatment with N-methyl-N′-nitro-N-nitrosoguanidine. The mutant was able to use neither glycerol nor l-α-glycerophosphate, nor maltose as carbon source. Enzyme and transport assays indicated that glycerol kinase and l-α-glycerophosphate permease were present. No activity of the cytochrome linked l-α-glycerophosphate dehydrogenase could be demonstrated. This activity was present in LT2 cells grown in the presence of glycerol. These results were interpreted as a glpD- character in the mutant. The inability to utilize maltose as carbon source was due to lack of the amylomaltase activity. The second enzyme needed for the utilization of maltose, maltodextrine phosphorylase, was present in mutant SM6 at normal levels. The mutant was thus malQ-. By conjugation, both affected loci were located at about minutes 111–112 on the bacterial chromosome. By transduction it was found that there was approximately a 20% linkage between the two affected loci.

Key words

Salmonella typhimurium Mutants malQ-glpD Linkage Maltose and Glycerol Metabolism 
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References

  1. Adelberg, E. A., Mandel, M., Ching-Chen, G. C.: Optimal conditions for mutangenesis by N-methyl-N′-nitro-N-nitrosoguanidine in Escherichia coli. Biochem. biophys. Res. Commun. 18, 788–800 (1965)Google Scholar
  2. Botstein, D., Jones, E. W.: Nonrandom mutagenesis of the Escherichia coli genome by nitrosoguanidine. J. Bact. 98, 847–848 (1969)Google Scholar
  3. Carrillo-Castañeda, G., Ortega, M. V.: Effect of inorganic phosphate upon Salmonella typhimurium phosphatase activities: non-repressible alkaline phosphatase and non-inhibited acid phosphatase. Biochim. biophys. Acta (Amst.) 146, 535–543 (1967)Google Scholar
  4. Carrillo-Castañeda, G., Ortega, M. V.: Mutants of Salmonella typhimurium lacking phosphoenolpyruvate carboxykinase and α-ketoglutarate dehydrogenase activities. J. Bact. 102, 524–530 (1970)Google Scholar
  5. Cerdá-Olmedo, E., Hanawalt, P. C., Guerola, N.: Mutagenesis of the replication point by nitrosoguanidine: map and pattern of replication of the Escherichia coli chromosome. J. molec. Biol. 33, 705–719 (1968)Google Scholar
  6. Cozzarelli, N. R., Freedberg, W. B., Lin, E. C. C.: Genetic control of the l-α-glycerophosphate system in Escherichia coli. J. molec. Biol. 31, 371–387 (1968)Google Scholar
  7. Cozzarelli, N. R., Koch, J. P., Hayashi, S., Lin, E. C. C.: Growth stasis by accumulated l-α-glycerophosphate in Escherichia coli. J. Bact. 90, 1325–1329 (1965)Google Scholar
  8. Cozzarelli, N. R., Lin, E. C. C.: Chromosomal location of the structural gene for glycerol kinase in Escherichia coli. J. Bact. 91, 1763–1766 (1966)Google Scholar
  9. Davis, B. D., Mingioli, E. S.: Mutants of Escherichia coli requiring methionine or vitamine B12. J. Bact. 60, 17–28 (1950)Google Scholar
  10. Eisenstark, A., Eisenstark, R., Van Sickle, R.: Mutation of Salmonella typhimurium by nitrosoguanidine. Mutation Res. 2, 1–10 (1965)Google Scholar
  11. Groves, W. E., Davis, F. C., Sells, B. H.: Spectrophotometric determination of microgram quantities of protein without nucleic acid interference. Analyt. Biochem. 22, 195–210 (1968)Google Scholar
  12. Guarneros, G., Ortega, M. V.: Cysteine desulfhydrase activities of Salmonella typhimurium and Escherichia coli. Biochim. biophys. Acta (Amst.) 198, 132–142 (1970)Google Scholar
  13. Hatfield, D., Hofnung, M., Schwartz, M.: Genetic analysis of the maltose A region in Escherichia coli. J. Bact. 98, 559–567 (1969a)Google Scholar
  14. Hatfield, D., Hofnung, M., Schwartz, M.: Nonsense mutations in the maltose A region of the genetic map of Escherichia coli. J. Bact. 100, 1311–1315 (1969b)Google Scholar
  15. Hayashi, S., Koch, J. P., Lin, E. C. C.: Active transport of l-α-glycerophosphate in Escherichia coli. J. biol. Chem. 239, 3098–3105 (1964)Google Scholar
  16. Hayashi, S., Lin, E. C. C.: Capture of glycerol by cells of Escherichia coli. Biochim. biophys. Acta (Amst.) 94, 479–487 (1965a)Google Scholar
  17. Hayashi, S., Lin, E. C.: Product induction of glycerol kinase in Escherichia coli. J. molec. Biol. 14, 515–521 (1965b)Google Scholar
  18. Hirota, Y., Jacob, F., Ryter, A., Buttin, G., Nakai, T.: On the process of cellular division in Escherichia coli. I. Asymmetrical division and production of deoxyribonucleic acid-less bacteria. J. molec. Biol. 35, 175–192 (1968)Google Scholar
  19. Hofnung, M., Schwartz, M., Hatfield, D.: Complementation studies in the maltose A region of the Escherichia coli K12 genetic map. J. molec. Biol. 61, 681–694 (1971)Google Scholar
  20. Koch, J. P., Hayashi, S., Lin, E. C. C.: The control of dissimilation of glycerol and l-α-glycerophosphate in Escherichia coli. J. biol. Chem. 239, 3106–3108 (1964)Google Scholar
  21. Lin, E. C. C., Koch, J. P., Chused, T. M., Jorgensen, S. E.: Utilization of l-α-glycerophosph by Escherichia coli without hydrolysis. Proc. nat. Acad. Sci. (Wash.) 48, 2145–2150 (1962)Google Scholar
  22. Parada, J. L., Ortega, M. V.: Growth inhibition by hexoses of a temperature-sensitive thiazoleless mutant of Salmonella typhimurium. J. Bact. 94, 707–711 (1967)Google Scholar
  23. Parada, J. L., Ortega, M. V., Carrillo-Castañeda, G.: Biochemical and genetic characteristics of the C4-dicarboxylic acids transport system of Salmonella typhimurium. Arch. Mikrobiol. 94, 65–76 (1973)Google Scholar
  24. Richey, D. P., Lin, E. C. C.: Importance of facilitated diffusion for effective utilization of glycerol by Escherichia coli. J. Bact. 112, 784–790 (1972)Google Scholar
  25. Sanderson, K. E.: Linkage map of Salmonella typhimurium, ed. IV. Bact. Rev. 36, 558–586 (1972)Google Scholar
  26. Sanderson, K. E., Ross, H., Ziegler, L., Mäkelä, P. H.: F+, Hfr, and F′ strains of Salmonella typhimurium and Salmonella abony. Bact. Rev. 36, 608–637 (1972)Google Scholar
  27. Sanno, Y., Wilson, T. H., Lin, E. C. C.: Control of permeation of glycerol in cells of Escherichia coli. Biochem. biophys. Res. Commun. 32, 344–349 (1968)Google Scholar
  28. Schwartz, M.: Location of the maltose A and B loci on the genetic map of Escherichia coli. J. Bact. 92, 1083–1089 (1966)Google Scholar
  29. Schwartz, M.: Expression phénotypique et localization génétique des mutations affectant le métabolisme du maltose chez Escherichia coli K12. Ann. Inst. Pasteur 112, 673–700 (1967a)Google Scholar
  30. Schwartz, M.: Sur lexistence chez Escherichia coli K12 d'une régulation commune a la biosynthese des récepteurs du bacteriophage λ et au métabolisme du maltose. Ann. Inst. Pasteur 113, 685–704 (1967b)Google Scholar
  31. Taylor, A. L., Trotter, C. D.: Linkage map of Escherichia coli strain K-12. Bact. Rev. 36, 504–524 (1972)Google Scholar
  32. Wiesmayer, M., Cohn, M.: The characterization of the pathway of maltose utilization by Escherichia coli. I. Purification and chamical properties of the enzyme amylomaltase. Biochim. biophys. Acta (Amst.) 39, 417–426 (1960a)Google Scholar
  33. Wiesmayer, M., Cohn, M.: The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase. Biochim. biophys. Acta (Amst.) 39, 427–439 (1960b)Google Scholar
  34. Wiesmayer, M., Cohn, M.: The characterization of the pathway of maltose utilization by Escherichia coli. III. A description of the concentrating mechanism. Biochim. biophys. Acta (Amst.) 39, 440–447 (1960c)Google Scholar

Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • Efraín Aceves-Piña
    • 1
  • Manuel V. Ortega
    • 1
  • Mireya Artís
    • 1
  1. 1.Departamento de GenéticaCentro de Investigación y de Estudios Avanzados del IPNMéxico

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