Summary
By two consecutive treatments with N-methyl-N′-nitro-N-nitrosoguanidine we obtained mutant SM151 of Salmonella typhimurium which differs from the parental LT2 strain in: a) is able to use l-glutamate as carbon source (first mutation), and b) requires that amino acid for growth (second mutation). It was found that the requirement of mutant SM151 for glutamate was due to a very low activity of glutamate dehydrogenase. Both glutamate-oxaloacetate transaminase and aspartase activities were present at normal levels. Glutamate dehydrogenase activity was strongly repressed by glutamate; aspartase activity was under severe catabolite (glucose) repression, while glutamate-oxaloacetate transaminase was partially repressed by glutamate. By conjugation and transduction the locus gdh, responsible for the low activity of the glutamate dehydrogenase of mutant SM151, was located at about minute 128 of the bacterial chromosome and found to be linked to the argC, argF, and metB loci.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Adelberg, E. A., Mandel, M., Ching-Chen, G. C.: Optimal conditions for mutagenesis by N-methyl-N′-nitro-N-nitrosoguanidine in E. coli K12. Biochem. biophys. Res. Commun. 18, 788–800 (1965)
Bergmeyer, H. U., Bernt, E.: Glutamate-oxaloacetate transaminase. Methods of enzymatic analysis (H. U. Bergmeyer, ed.), p. 837–842. New York-London: Academic Press 1965
Davis, B. D., Mingioli, E. S.: Mutants of Escherichia coli requiring methionine or vitamin B12. J. Bact. 60, 17–28 (1950)
Gilvarg, C., Davis, B. D.: The role of the tricarboxylic acid cycle in acetate oxidation in Escherichia coli. J. biol. Chem. 222, 307–319 (1956)
Groves, W. E., Davis, F. C., Jr., Sells, B. H.: Spectrophotometric determination of microgram quantities of protein without nucleic acid interference. Analyt. Biochem. 22, 195–210 (1968)
Halpern, Y. S., Lupo, M.: Glutamate transport in wild-type and mutant strains of Escherichia coli. J. Bact. 90, 1288–1295 (1965)
Halpern, Y. S., Umbarger, H. E.: Conversion of ammonia to amino groups in Escherichia coli. J. Bact. 80, 285–288 (1960)
LéJohn, H. B.: Unidirectional inhibition of glutamate dehydrogenase by metabolites. J. biol. Chem. 243, 5126–5131 (1968)
Marcus, M., Halpern, Y. S.: The metabolic pathway of glutamate in Escherichia coli. Biochim. biophys. Acta (Amst.) 177, 314–320 (1969).
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)
Sanderson, K. E.: Linkage map of Salmonella typhimurium, Edition IV. Bact. Rev. 36, 558–586 (1972)
Sanderson, K. E., Demerec, M.: The linkage map of Salmonella typhimurium. Genetics 51, 897–913 (1965)
Vender, J., Rickenberg, H. V.: Ammonia metabolism in a mutant of Escherichia coli lacking glutamate dehydrogenase. Biochim. biophys. Acta (Amst.) 90, 218–220 (1964)
Williams, V. R., Lartigne, D. J.: Quarternary structure and certain allosteric properties of aspartase. J. biol. Chem. 242, 2973–2978 (1967)
Author information
Authors and Affiliations
Additional information
Communicated by W. Maas
Rights and permissions
About this article
Cite this article
Ortega, M.V., Aguilar, C. Biochemical and genetic characterization of a mutant of Salmonella typhimurium defective in a locus for glutamate dehydrogenase activity. Molec. Gen. Genet. 125, 351–358 (1973). https://doi.org/10.1007/BF00276590
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00276590