Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1970 Jun;102(3):804–809. doi: 10.1128/jb.102.3.804-809.1970

Mechanisms of Lactose Utilization by Lactic Acid Streptococci: Enzymatic and Genetic Analyses1

L McKay a,2, A Miller III a, W E Sandine a, P R Elliker a
PMCID: PMC247630  PMID: 5429725

Abstract

The apparent instability of β-galactosidase in toluene-treated cells or cell-free extracts of lactic streptococci is explained by the fact that these organisms do not contain the expected enzyme. Instead, various strains of Streptococcus lactis, S. cremoris, and S. diacetilactis were shown to hydrolyze o-nitrophenyl-β-d-galactoside-6-phosphate (ONPG-6-P), indicating the presence of a different enzyme. In addition, lactose metabolism in S. lactis C2F was found to involve enzyme I (EI), enzyme II (EII), factor III (FIII), and a heat-stable protein (HPr) of a phosphoenolpyruvate (PEP)-dependent phosphotransferase system analogous to that of Staphylococcus aureus. Mutants of S. lactis C2F, defective in lactose metabolism, possessed the phenotype lac− gal−. These strains were unable to accumulate 14C-thiomethyl-β-d-galactoside, to hydrolyze ONPG, or to utilize lactose when grown in lactose or galactose broth. In addition, these mutants contained EI and HPr, but lacked EII, FIII, and the ability to hydrolyze ONPG-6-P. This suggested that the defect was in the phosphorylation step. Lactose-negative mutants of S. lactis 7962, a strain containing β-galactosidase, could be separated into several classes, which indicated that this organism is not dependent upon the PEP-phosphotransferase system for lactose metabolism.

Full text

PDF
804

Selected References

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

  1. CITTI J. E., SANDINE W. E., ELLIKER P. R. BETA-GALACTOSIDASE OF STREPTOCOCCUS LACTIS. J Bacteriol. 1965 Apr;89:937–942. doi: 10.1128/jb.89.4.937-942.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. EATON N. R. New press for disruption of microorganisms. J Bacteriol. 1962 Jun;83:1359–1360. doi: 10.1128/jb.83.6.1359-1360.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hengstenberg W., Egan J. B., Morse M. L. Carbohydrate transport in Staphylococcus aureus. V. The accumulation of phosphorylated carbohydrate derivatives, and evidence for a new enzyme-splitting lactose phosphate. Proc Natl Acad Sci U S A. 1967 Jul;58(1):274–279. doi: 10.1073/pnas.58.1.274. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hengstenberg W., Egan J. B., Morse M. L. Carbohydrate transport in Staphylococcus aureus. VI. The nature of the derivatives accumulated. J Biol Chem. 1968 Apr 25;243(8):1881–1885. [PubMed] [Google Scholar]
  5. Hengstenberg W., Penberthy W. K., Hill K. L., Morse M. L. Metabolism of lactose by Staphylococcus aureus. J Bacteriol. 1968 Dec;96(6):2187–2188. doi: 10.1128/jb.96.6.2187-2188.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hengstenberg W., Penberthy W. K., Hill K. L., Morse M. L. Phosphotransferase system of Staphylococcus aureus: its requirement for the accumulation and metabolism of galactosides. J Bacteriol. 1969 Aug;99(2):383–388. doi: 10.1128/jb.99.2.383-388.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hirota Y. THE EFFECT OF ACRIDINE DYES ON MATING TYPE FACTORS IN ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1960 Jan;46(1):57–64. doi: 10.1073/pnas.46.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. JACOB F., MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318–356. doi: 10.1016/s0022-2836(61)80072-7. [DOI] [PubMed] [Google Scholar]
  9. KUNDIG W., GHOSH S., ROSEMAN S. PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEM. Proc Natl Acad Sci U S A. 1964 Oct;52:1067–1074. doi: 10.1073/pnas.52.4.1067. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kennedy E. P., Scarborough G. A. Mechanism of hydrolysis of O-nitrophenyl-beta-galactoside in Staphylococcus aureus and its significance for theories of sugar transport. Proc Natl Acad Sci U S A. 1967 Jul;58(1):225–228. doi: 10.1073/pnas.58.1.225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Laue P., MacDonald R. E. Identification of thiomethyl-beta-D-galactoside 6-phosphate accumulated by Staphylococcus aureus. J Biol Chem. 1968 Feb 10;243(3):680–682. [PubMed] [Google Scholar]
  12. McKay L. L., Walter L. A., Sandine W. E., Elliker P. R. Involvement of phosphoenolpyruvate in lactose utilization by group N streptococci. J Bacteriol. 1969 Aug;99(2):603–610. doi: 10.1128/jb.99.2.603-610.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Morse M. L., Hill K. L., Egan J. B., Hengstenberg W. Metabolism of lactose by Staphylococcus aureus and its genetic basis. J Bacteriol. 1968 Jun;95(6):2270–2274. doi: 10.1128/jb.95.6.2270-2274.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Simoni R. D., Smith M. F., Roseman S. Resolution of a staphylococcal phosphotransferase system into four protein components and its relation to sugar transport. Biochem Biophys Res Commun. 1968 Jun 10;31(5):804–811. doi: 10.1016/0006-291x(68)90634-7. [DOI] [PubMed] [Google Scholar]
  15. Tanaka S., Lin E. C. Two classes of pleiotropic mutants of Aerobacter aerogenes lacking components of a phosphoenolpyruvate-dependent phosphotransferase system. Proc Natl Acad Sci U S A. 1967 Apr;57(4):913–919. doi: 10.1073/pnas.57.4.913. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES