Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1976 Oct;128(1):86–98. doi: 10.1128/jb.128.1.86-98.1976

Mutant strains (nit) of Salmonella typhimurium with a pleiotropic defect in nitrogen metabolism.

J Broach, C Neumann, S Kustu
PMCID: PMC232829  PMID: 10275

Abstract

We have isolated mutant strains (nit) of Salmonella typhimurium that are defective in nitrogen metabolism. They have a reduced ability to use a variety of compounds including glutamate, proline, arginine, N-acetyl-glucosamine, alanine, and adenosine as sole nitrogen source. In addition, although they grow normally on high concentrations of ammonium chloride (greater than 1 mM) as nitrogen source, they grow substantially more slowly than wild type at low concentrations (less than 1 mM). We postulated that the inability of these strains to utilize low concentrations of ammonium chloride accounts for their poor growth on other nitrogen sources. The specific biochemical lesion in strains with a nit mutation is not known; however, mutant strains have no detectable alteration in the activities of glutamine synthetase, glutamate synthetase, or glutamate dehydrogenase, the enzymes known to be involved in assimilation of ammonia. A nit mutation is suppressed by second-site mutations in the structural gene for glutamine synthetase (glnA) that decrease glutamine synthetase activity.

Full text

PDF
86

Selected References

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

  1. AMES G. F. UPTAKE OF AMINO ACIDS BY SALMONELLA TYPHIMURIUM. Arch Biochem Biophys. 1964 Jan;104:1–18. doi: 10.1016/s0003-9861(64)80028-x. [DOI] [PubMed] [Google Scholar]
  2. Alper M. D., Ames B. N. Positive selection of mutants with deletions of the gal-chl region of the Salmonella chromosome as a screening procedure for mutagens that cause deletions. J Bacteriol. 1975 Jan;121(1):259–266. doi: 10.1128/jb.121.1.259-266.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brenchley J. E., Baker C. A., Patil L. G. Regulation of the ammonia assimilatory enzymes in Salmonella typhimurium. J Bacteriol. 1975 Oct;124(1):182–189. doi: 10.1128/jb.124.1.182-189.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brenchley J. E., Prival M. J., Magasanik B. Regulation of the synthesis of enzymes responsible for glutamate formation in Klebsiella aerogenes. J Biol Chem. 1973 Sep 10;248(17):6122–6128. [PubMed] [Google Scholar]
  5. Dendinger S., Brill W. J. Regulation of proline degradation in Salmonella typhimurium. J Bacteriol. 1970 Jul;103(1):144–152. doi: 10.1128/jb.103.1.144-152.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Enomoto M., Stocker B. A. Transduction by phage P1kc in Salmonella typhimurium. Virology. 1974 Aug;60(2):503–514. doi: 10.1016/0042-6822(74)90344-4. [DOI] [PubMed] [Google Scholar]
  7. Ginsburg A., Yeh J., Hennig S. B., Denton M. D. Some effects of adenylylation on the biosynthetic properties of the glutamine synthetase from Escherichia coli. Biochemistry. 1970 Feb 3;9(3):633–649. doi: 10.1021/bi00805a025. [DOI] [PubMed] [Google Scholar]
  8. HALPERN Y. S., UMBARGER H. E. Conversion of ammonia to amino groups in Escherichia coli. J Bacteriol. 1960 Sep;80:285–288. doi: 10.1128/jb.80.3.285-288.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. HALPERN Y. S., UMBARGER H. E. Utilization of L-glutamic and 2-oxoglutaric acid as sole sources of carbon by Escherichia coli. J Gen Microbiol. 1961 Oct;26:175–183. doi: 10.1099/00221287-26-2-175. [DOI] [PubMed] [Google Scholar]
  10. Halpern Y. S., Lupo M. Glutamate transport in wild-type and mutant strains of Escherichia coli. J Bacteriol. 1965 Nov;90(5):1288–1295. doi: 10.1128/jb.90.5.1288-1295.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jackson E. N., Yanofsky C. Localization of two functions of the phosphoribosyl anthranilate transferase of Escherichia coli to distinct regions of the polypeptide chain. J Bacteriol. 1974 Feb;117(2):502–508. doi: 10.1128/jb.117.2.502-508.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kingdon H. S., Shapiro B. M., Stadtman E. R. Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1703–1710. doi: 10.1073/pnas.58.4.1703. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kustu S. G., Ames G. F. The hisP protein, a known histidine transport component in Salmonella typhimurium, is also an arginine transport component. J Bacteriol. 1973 Oct;116(1):107–113. doi: 10.1128/jb.116.1.107-113.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kustu S. G., McKereghan K. Mutations affecting glutamine synthetase activity in Salmonella typhimurium. J Bacteriol. 1975 Jun;122(3):1006–1016. doi: 10.1128/jb.122.3.1006-1016.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. Marcus M., Halpern Y. S. The metabolic pathway of glutamate in Escherichia coli K-12. Biochim Biophys Acta. 1969 Apr 1;177(2):314–320. doi: 10.1016/0304-4165(69)90141-x. [DOI] [PubMed] [Google Scholar]
  17. Mecke D., Holzer H. Repression und inaktivierung von Glutaminsynthetase in Escherichia coli durch NH4+. Biochim Biophys Acta. 1966 Aug 10;122(2):341–351. [PubMed] [Google Scholar]
  18. Meers J. L., Tempest D. W., Brown C. M. 'Glutamine(amide):2-oxoglutarate amino transferase oxido-reductase (NADP); an enzyme involved in the synthesis of glutamate by some bacteria. J Gen Microbiol. 1970 Dec;64(2):187–194. doi: 10.1099/00221287-64-2-187. [DOI] [PubMed] [Google Scholar]
  19. Miller R. E., Stadtman E. R. Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein. J Biol Chem. 1972 Nov 25;247(22):7407–7419. [PubMed] [Google Scholar]
  20. Nagatani H., Shimizu M., Valentine R. C. The mechanism of ammonia assimilation in nitrogen fixing Bacteria. Arch Mikrobiol. 1971;79(2):164–175. doi: 10.1007/BF00424923. [DOI] [PubMed] [Google Scholar]
  21. Ornellas E. P., Stocker B. A. Relation of lipopolysaccharide character to P1 sensitivity in Salmonella typhimurium. Virology. 1974 Aug;60(2):491–502. doi: 10.1016/0042-6822(74)90343-2. [DOI] [PubMed] [Google Scholar]
  22. Prival M. J., Brenchley J. E., Magasanik B. Glutamine synthetase and the regulation of histidase formation in Klebsiella aerogenes. J Biol Chem. 1973 Jun 25;248(12):4334–4344. [PubMed] [Google Scholar]
  23. Prival M. J., Magasanik B. Resistance to catabolite repression of histidase and proline oxidase during nitrogen-limited growth of Klebsiella aerogenes. J Biol Chem. 1971 Oct 25;246(20):6288–6296. [PubMed] [Google Scholar]
  24. Sanderson K. E., Ross H., Ziegler L., Mäkelä P. H. F + , Hfr, and F' strains of Salmonella typhimurium and Salmonella abony. Bacteriol Rev. 1972 Dec;36(4):608–637. doi: 10.1128/br.36.4.608-637.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Schmieger H. A method for detection of phage mutants with altered transducing ability. Mol Gen Genet. 1971;110(4):378–381. doi: 10.1007/BF00438281. [DOI] [PubMed] [Google Scholar]
  26. Shapiro B. M., Kingdon H. S., Stadtman E. R. Regulation of glutamine synthetase. VII. Adenylyl glutamine synthetase: a new form of the enzyme with altered regulatory and kinetic properties. Proc Natl Acad Sci U S A. 1967 Aug;58(2):642–649. doi: 10.1073/pnas.58.2.642. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Smith H. O., Levine M. A phage P22 gene controlling integration of prophage. Virology. 1967 Feb;31(2):207–216. doi: 10.1016/0042-6822(67)90164-x. [DOI] [PubMed] [Google Scholar]
  28. Stadtman E. R., Ginsburg A., Ciardi J. E., Yeh J., Hennig S. B., Shapiro B. M. Multiple molecular forms of glutamine synthetase produced by enzyme catalyzed adenylation and deadenylylation reactions. Adv Enzyme Regul. 1970;8:99–118. doi: 10.1016/0065-2571(70)90011-7. [DOI] [PubMed] [Google Scholar]
  29. Steimer-Veale K., Brenchley J. E. Characterization of Salmonella typhimurium strains sensitive and resistant to methionine sulfoximine. J Bacteriol. 1974 Sep;119(3):848–856. doi: 10.1128/jb.119.3.848-856.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Tiemeier D. C., Milman G. Chinese hamster liver glutamine synthetase. Purification, physical and biochemical properties. J Biol Chem. 1972 Apr 25;247(8):2272–2277. [PubMed] [Google Scholar]
  31. Trotta P. P., Platzer K. E., Haschemeyer R. H., Meister A. Glutamine-binding subunit of glutamate synthase and partial reactions catalyzed by this glutamine amidotransferase. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4607–4611. doi: 10.1073/pnas.71.11.4607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Tubb R. S. Glutamine synthetase and ammonium regulation of nitrogenase synthesis in Klebsiella. Nature. 1974 Oct 11;251(5475):481–485. doi: 10.1038/251481a0. [DOI] [PubMed] [Google Scholar]
  33. Tyler B., Deleo A. B., Magasanik B. Activation of transcription of hut DNA by glutamine synthetase. Proc Natl Acad Sci U S A. 1974 Jan;71(1):225–229. doi: 10.1073/pnas.71.1.225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  35. Woolfolk C. A., Shapiro B., Stadtman E. R. Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli. Arch Biochem Biophys. 1966 Sep 26;116(1):177–192. doi: 10.1016/0003-9861(66)90026-9. [DOI] [PubMed] [Google Scholar]
  36. Zalkin H., Murphy T. Utilization of ammonia for tryptophan synthesis. Biochem Biophys Res Commun. 1975 Dec 15;67(4):1370–1377. doi: 10.1016/0006-291x(75)90178-3. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES