Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1975 Mar;121(3):1078–1084. doi: 10.1128/jb.121.3.1078-1084.1975

Isolation and characterization of D-serine deaminase constitutive mutants by utilization of D-serine as sole carbon or nitrogen source.

F R Bloom, E McFall
PMCID: PMC246038  PMID: 1090588

Abstract

Mutants constitutive for D-serine deaminase (Dsdase) synthesis were isolated by utilizing D-serine as sole nitrogen or carbon source in the chemostat. This method generated only regulatory constitutive (dsdC) mutants. The altered dsdC gene product in these strains is apparently able to bind D-serine more efficiently than the wild-type dsdC+ gene product--a selective advantage. Constitutive synthesis of Dsdase in all of these dsdC mutants is extremely sensitive to catabolite repression, and catabolite repression is reversed by the addition of D-serine. Of the 15 mutants generated by this method, none are suppressible by supD, supE, or supF. Mutations to a low level of constitutivity (maximal specific activity of 9) occur much more frequently than mutations to a high level (maximal specific activity of 79). High level constitutive synthesis of Dsdase results from the synthesis of an altered dsdC gene product--not from loss of ability to form the dsdC product. Dsdase synthesis is not regulated by the nitrogen supply in the medium, as nitrogen starvation does not result in the derepression of Dsdase synthesis.

Full text

PDF
1078

Selected References

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

  1. Bloom F. R., McFall E., Young M. C., Carothers A. M. Positive control in the D-serine deaminase system of Escherichia coli K-12. J Bacteriol. 1975 Mar;121(3):1092–1101. doi: 10.1128/jb.121.3.1092-1101.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cosloy S. D., McFall E. Metabolism of D-serine in Escherichia coli K-12: mechanism of growth inhibition. J Bacteriol. 1973 May;114(2):685–694. doi: 10.1128/jb.114.2.685-694.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dupourque D., Newton W. A., Snell E. E. Purification and properties of D-serine dehydrase from Escherichia coli. J Biol Chem. 1966 Mar 10;241(5):1233–1238. [PubMed] [Google Scholar]
  4. Englesberg E., Irr J., Power J., Lee N. Positive control of enzyme synthesis by gene C in the L-arabinose system. J Bacteriol. 1965 Oct;90(4):946–957. doi: 10.1128/jb.90.4.946-957.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. LURIA S. E., ADAMS J. N., TING R. C. Transduction of lactose-utilizing ability among strains of E. coli and S. dysenteriae and the properties of the transducing phage particles. Virology. 1960 Nov;12:348–390. doi: 10.1016/0042-6822(60)90161-6. [DOI] [PubMed] [Google Scholar]
  6. MANDELSTAM J. The repression of constitutive beta-galactosidase in Escherichia coli by glucose and other carbon sources. Biochem J. 1962 Mar;82:489–493. doi: 10.1042/bj0820489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. MCFALL E. GENETIC STRUCTURE OF THE D-SERINE DEAMINASE SYSTEM OF ESCHERICHIA COLI. J Mol Biol. 1964 Sep;9:746–753. doi: 10.1016/s0022-2836(64)80179-0. [DOI] [PubMed] [Google Scholar]
  8. MCFALL E. PLEIOTROPIC MUTATIONS IN THE D-SERINE DEAMINASE SYSTEM OF ESCHERICHIA COLI. J Mol Biol. 1964 Sep;9:754–762. doi: 10.1016/s0022-2836(64)80180-7. [DOI] [PubMed] [Google Scholar]
  9. Magasanik B., Prival M. J., Brenchley J. E., Tyler B. M., DeLeo A. B., Streicher S. L., Bender R. A., Paris C. G. Glutamine synthetase as a regulator of enzyme synthesis. Curr Top Cell Regul. 1974;8(0):119–138. doi: 10.1016/b978-0-12-152808-9.50010-9. [DOI] [PubMed] [Google Scholar]
  10. McFall E. Dominance studies with stable merodiploids in the D-serine deaminase system of Escherichia coli K-12. J Bacteriol. 1967 Dec;94(6):1982–1988. doi: 10.1128/jb.94.6.1982-1988.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. McFall E. Escherichia coli K-12 mutant forming a temperature-sensitive D-serine deaminase. J Bacteriol. 1975 Mar;121(3):1074–1077. doi: 10.1128/jb.121.3.1074-1077.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McFall E. Mapping of the d-serine deaminase region in Escherichia coli K-12. Genetics. 1967 Jan;55(1):91–99. doi: 10.1093/genetics/55.1.91. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. NOVICK A., SZILARD L. Experiments with the Chemostat on spontaneous mutations of bacteria. Proc Natl Acad Sci U S A. 1950 Dec;36(12):708–719. doi: 10.1073/pnas.36.12.708. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. STACEY K. A., SIMSON E. IMPROVED METHOD FOR THE ISOLATION OF THYMINE-REQUIRING MUTANTS OF ESCHERICHIA COLI. J Bacteriol. 1965 Aug;90:554–555. doi: 10.1128/jb.90.2.554-555.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES