Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1989 Jun;171(6):2942–2948. doi: 10.1128/jb.171.6.2942-2948.1989

Concentration-dependent repression of the soluble and membrane components of the Streptococcus mutans phosphoenolpyruvate: sugar phosphotransferase system by glucose.

I R Hamilton 1, L Gauthier 1, B Desjardins 1, C Vadeboncoeur 1
PMCID: PMC209998  PMID: 2722738

Abstract

Growth of Streptococcus mutans Ingbritt in continuous culture (pH 7.0, dilution rate of 0.1 h-1) at medium glucose concentrations above 2.6 mM resulted in repression of the sugar-specific membrane components, enzyme IIGlc (EIIGlc) and EIIMan, of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). In one experiment, significant repression (27-fold) was observed with 73 mM glucose when the glycolytic capacity of the cells was reduced by only 2-fold and when the culture was still glucose limited. In a more comprehensive experiment in which cells were grown in continuous culture at eight glucose concentrations from 2.6 to 304 mM, in addition to repression of specific EII activities for glucose, mannose, 2-deoxyglucose, and fructose, synthesis of the general protein, EI, was repressed at all glucose levels above 2.6 mM to a maximum of 4-fold at 304 mM glucose when the culture was growing with excess glucose (i.e., nitrogen limited). The other PTS general protein, HPr, was less sensitive to the exogenous glucose level but was nevertheless repressed fourfold under glucose-excess conditions. The Km for glucose for EIIGlc increased from 0.22 mM during growth at 3.6 mM glucose (glucose limited) to 0.48 mM at 271 mM glucose (glucose excess). The shift from heterofermentation to homofermentation during growth with increasing glucose levels suggests the involvement of glycolytic intermediates, ATP, or another high-energy phosphate metabolite in regulation of the synthesis of the PTS components in S. mutans.

Full text

PDF
2942

Selected References

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

  1. Bowden G. H., Hardie J. M., Fillery E. D. Antigens from Actinomyces species and their value in identification. J Dent Res. 1976 Jan;55:A192–A204. doi: 10.1177/002203457605500112011. [DOI] [PubMed] [Google Scholar]
  2. Calmes R. Involvement of phosphoenolpyruvate in the catabolism of caries-conducive disaccharides by Streptococcus mutans: lactose transport. Infect Immun. 1978 Mar;19(3):934–942. doi: 10.1128/iai.19.3.934-942.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dykhuizen D., Hartl D. Transport by the lactose permease of Escherichia coli as the basis of lactose killing. J Bacteriol. 1978 Sep;135(3):876–882. doi: 10.1128/jb.135.3.876-882.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ellwood D. C., Hamilton I. R. Properties of Streptococcus mutans Ingbritt growing on limiting sucrose in a chemostat: repression of the phosphoenolpyruvate phosphotransferase transport system. Infect Immun. 1982 May;36(2):576–581. doi: 10.1128/iai.36.2.576-581.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ellwood D. C., Phipps P. J., Hamilton I. R. Effect of growth rate and glucose concentration on the activity of the phosphoenolpyruvate phosphotransferase system in Streptococcus mutans Ingbritt grown in continuous culture. Infect Immun. 1979 Feb;23(2):224–231. doi: 10.1128/iai.23.2.224-231.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gachelin G. Studies on the alpha-methylglucoside permease of Escherichia coli. A two-step mechanism for the accumulation of alpha-methylglucoside 6-phosphate. Eur J Biochem. 1970 Oct;16(2):342–357. doi: 10.1111/j.1432-1033.1970.tb01088.x. [DOI] [PubMed] [Google Scholar]
  7. Gauthier L., Mayrand D., Vadeboncoeur C. Isolation of a novel protein involved in the transport of fructose by an inducible phosphoenolpyruvate fructose phosphotransferase system in Streptococcus mutans. J Bacteriol. 1984 Nov;160(2):755–763. doi: 10.1128/jb.160.2.755-763.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hamilton I. R., Bowden G. H. Response of freshly isolated strains of Streptococcus mutans and Streptococcus mitior to change in pH in the presence and absence of fluoride during growth in continuous culture. Infect Immun. 1982 Apr;36(1):255–262. doi: 10.1128/iai.36.1.255-262.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hamilton I. R., Ellwood D. C. Effects of fluoride on carbohydrate metabolism by washed cells of Streptococcus mutans grown at various pH values in a chemostat. Infect Immun. 1978 Feb;19(2):434–442. doi: 10.1128/iai.19.2.434-442.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hamilton I. R., Lo G. C. Co-induction of beta-galactosidase and the lactose-P-enolpyruvate phosphotransferase system in Streptococcus salivarius and Streptococcus mutans. J Bacteriol. 1978 Dec;136(3):900–908. doi: 10.1128/jb.136.3.900-908.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hamilton I. R., St Martin E. J. Evidence for the involvement of proton motive force in the transport of glucose by a mutant of Streptococcus mutans strain DR0001 defective in glucose-phosphoenolpyruvate phosphotransferase activity. Infect Immun. 1982 May;36(2):567–575. doi: 10.1128/iai.36.2.567-575.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Keevil C. W., McDermid A. S., Marsh P. D., Ellwood D. C. Protonmotive force driven 6-deoxyglucose uptake by the oral pathogen, Streptococcus mutans Ingbritt. Arch Microbiol. 1986 Nov;146(2):118–124. doi: 10.1007/BF00402337. [DOI] [PubMed] [Google Scholar]
  13. Liberman E. S., Bleiweis A. S. Role of the phosphoenolpyruvate-dependent glucose phosphotransferase system of Streptococcus mutans GS5 in the regulation of lactose uptake. Infect Immun. 1984 Feb;43(2):536–542. doi: 10.1128/iai.43.2.536-542.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Loesche W. J. Role of Streptococcus mutans in human dental decay. Microbiol Rev. 1986 Dec;50(4):353–380. doi: 10.1128/mr.50.4.353-380.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. London J., Hausman S. Xylitol-mediated transient inhibition of ribitol utilization by Lactobacillus casei. J Bacteriol. 1982 May;150(2):657–661. doi: 10.1128/jb.150.2.657-661.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Postma P. W., Lengeler J. W. Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria. Microbiol Rev. 1985 Sep;49(3):232–269. doi: 10.1128/mr.49.3.232-269.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rodrigue L., Lacoste L., Trahan L., Vadeboncoeur C. Effect of nutritional constraints on the biosynthesis of the components of the phosphoenolpyruvate: sugar phosphotransferase system in a fresh isolate of Streptococcus mutans. Infect Immun. 1988 Feb;56(2):518–522. doi: 10.1128/iai.56.2.518-522.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schachtele C. F., Mayo J. A. Phosphoenolpyruvate-dependent glucose transport in oral streptococci. J Dent Res. 1973 Nov-Dec;52(6):1209–1215. doi: 10.1177/00220345730520060801. [DOI] [PubMed] [Google Scholar]
  19. St Martin E. J., Wittenberger C. L. Characterization of a phosphoenolpyruvate-dependent sucrose phosphotransferase system in Streptococcus mutans. Infect Immun. 1979 Jun;24(3):865–868. doi: 10.1128/iai.24.3.865-868.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Thibault L., Vadeboncoeur C. Phosphoenolpyruvate-sugar phosphotransferase transport system of Streptococcus mutans: purification of HPr and enzyme I and determination of their intracellular concentrations by rocket immunoelectrophoresis. Infect Immun. 1985 Dec;50(3):817–825. doi: 10.1128/iai.50.3.817-825.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Thompson J., Chassy B. M. Regulation of glycolysis and sugar phosphotransferase activities in Streptococcus lactis: growth in the presence of 2-deoxy-D-glucose. J Bacteriol. 1983 May;154(2):819–830. doi: 10.1128/jb.154.2.819-830.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Vadeboncoeur C., Gauthier L. The phosphoenolpyruvate: sugar phosphotransferase system of Streptococcus salivarius. Identification of a IIIman protein. Can J Microbiol. 1987 Feb;33(2):118–122. doi: 10.1139/m87-020. [DOI] [PubMed] [Google Scholar]
  23. Vadeboncoeur C., Proulx M. Lactose transport in Streptococcus mutans: isolation and characterization of factor IIIlac, a specific protein component of the phosphoenolpyruvate-lactose phosphotransferase system. Infect Immun. 1984 Oct;46(1):213–219. doi: 10.1128/iai.46.1.213-219.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Vadeboncoeur C., Proulx M., Trahan L. Purification of proteins similar to HPr and enzyme I from the oral bacterium Streptococcus salivarius. Biochemical and immunochemical properties. Can J Microbiol. 1983 Dec;29(12):1694–1705. doi: 10.1139/m83-260. [DOI] [PubMed] [Google Scholar]
  25. Vadeboncoeur C. Structure and properties of the phosphoenolpyruvate: glucose phosphotransferase system of oral streptococci. Can J Microbiol. 1984 Apr;30(4):495–502. doi: 10.1139/m84-073. [DOI] [PubMed] [Google Scholar]
  26. Vadeboncoeur C., Thibault L., Neron S., Halvorson H., Hamilton I. R. Effect of growth conditions on levels of components of the phosphoenolpyruvate:sugar phosphotransferase system in Streptococcus mutans and Streptococcus sobrinus grown in continuous culture. J Bacteriol. 1987 Dec;169(12):5686–5691. doi: 10.1128/jb.169.12.5686-5691.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Vadeboncoeur C., Trahan L. Glucose transport in Streptococcus salivarius. Evidence for the presence of a distinct phosphoenolpyruvate: glucose phosphotransferase system which catalyses the phosphorylation of alpha-methyl glucoside. Can J Microbiol. 1982 Feb;28(2):190–199. doi: 10.1139/m82-025. [DOI] [PubMed] [Google Scholar]
  28. ten Brink B., Otto R., Hansen U. P., Konings W. N. Energy recycling by lactate efflux in growing and nongrowing cells of Streptococcus cremoris. J Bacteriol. 1985 Apr;162(1):383–390. doi: 10.1128/jb.162.1.383-390.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES