Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1992 Oct;174(19):6152–6158. doi: 10.1128/jb.174.19.6152-6158.1992

Streptococcus mutans serotype c tagatose 6-phosphate pathway gene cluster.

E K Jagusztyn-Krynicka 1, J B Hansen 1, V L Crow 1, T D Thomas 1, A L Honeyman 1, R Curtiss 3rd 1
PMCID: PMC207682  PMID: 1328153

Abstract

DNA cloned into Escherichia coli K-12 from a serotype c strain of Streptococcus mutans encodes three enzyme activities for galactose utilization via the tagatose 6-phosphate pathway: galactose 6-phosphate isomerase, tagatose 6-phosphate kinase, and tagatose-1,6-bisphosphate aldolase. The genes coding for the tagatose 6-phosphate pathway were located on a 3.28-kb HindIII DNA fragment. Analysis of the tagatose proteins expressed by recombinant plasmids in minicells was used to determine the sizes of the various gene products. Mutagenesis of these plasmids with transposon Tn5 was used to determine the order of the tagatose genes. Tagatose 6-phosphate isomerase appears to be composed of 14- and 19-kDa subunits. The sizes of the kinase and aldolase were found to be 34 and 36 kDa, respectively. These values correspond to those reported previously for the tagatose pathway enzymes in Staphylococcus aureus and Lactococcus lactis.

Full text

PDF
6152

Images in this article

6155Image
on p.6155
6156Image
on p.6156

Selected References

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

  1. Alpert C. A., Chassy B. M. Molecular cloning and DNA sequence of lacE, the gene encoding the lactose-specific enzyme II of the phosphotransferase system of Lactobacillus casei. Evidence that a cysteine residue is essential for sugar phosphorylation. J Biol Chem. 1990 Dec 25;265(36):22561–22568. [PubMed] [Google Scholar]
  2. Alton N. K., Vapnek D. Nucleotide sequence analysis of the chloramphenicol resistance transposon Tn9. Nature. 1979 Dec 20;282(5741):864–869. doi: 10.1038/282864a0. [DOI] [PubMed] [Google Scholar]
  3. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bissett D. L., Anderson R. L. Lactose and D0galactose metabolism in Staphylococcus aureus: pathway of D-galactose 6-phosphate degradation. Biochem Biophys Res Commun. 1973 May 15;52(2):641–647. doi: 10.1016/0006-291x(73)90761-4. [DOI] [PubMed] [Google Scholar]
  5. Breidt F., Jr, Stewart G. C. Cloning and expression of the phospho-beta-galactosidase gene of Staphylococcus aureus in Escherichia coli. J Bacteriol. 1986 Jun;166(3):1061–1066. doi: 10.1128/jb.166.3.1061-1066.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chang A. C., Cohen S. N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol. 1978 Jun;134(3):1141–1156. doi: 10.1128/jb.134.3.1141-1156.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Crow V. L., Davey G. P., Pearce L. E., Thomas T. D. Plasmid linkage of the D-tagatose 6-phosphate pathway in Streptococcus lactis: effect on lactose and galactose metabolism. J Bacteriol. 1983 Jan;153(1):76–83. doi: 10.1128/jb.153.1.76-83.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Crow V. L., Thomas T. D. D-tagatose 1,6-diphosphate aldolase from lactic streptococci: purification, properties, and use in measuring intracellular tagatose 1,6-diphosphate. J Bacteriol. 1982 Aug;151(2):600–608. doi: 10.1128/jb.151.2.600-608.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Curtiss R., 3rd Genetic analysis of Streptococcus mutans virulence. Curr Top Microbiol Immunol. 1985;118:253–277. doi: 10.1007/978-3-642-70586-1_14. [DOI] [PubMed] [Google Scholar]
  10. De Vos W. M., Gasson M. J. Structure and expression of the Lactococcus lactis gene for phospho-beta-galactosidase (lacG) in Escherichia coli and L. lactis. J Gen Microbiol. 1989 Jul;135(7):1833–1846. doi: 10.1099/00221287-135-7-1833. [DOI] [PubMed] [Google Scholar]
  11. Frazer A. C., Curtiss R., 3rd Production, properties and utility of bacterial minicells. Curr Top Microbiol Immunol. 1975;69:1–84. doi: 10.1007/978-3-642-50112-8_1. [DOI] [PubMed] [Google Scholar]
  12. Hamada S., Slade H. D. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol Rev. 1980 Jun;44(2):331–384. doi: 10.1128/mr.44.2.331-384.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hamilton I. R., Lebtag H. Lactose metabolism by Streptococcus mutans: evidence for induction of the tagatose 6-phosphate pathway. J Bacteriol. 1979 Dec;140(3):1102–1104. doi: 10.1128/jb.140.3.1102-1104.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hansen J. B., Abiko Y., Curtiss R., 3rd Characterization of the Streptococcus mutans plasmid pva318 cloned into Escherichia coli. Infect Immun. 1981 Mar;31(3):1034–1043. doi: 10.1128/iai.31.3.1034-1043.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Honeyman A. L., Curtiss R., 3rd Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system. Infect Immun. 1992 Aug;60(8):3369–3375. doi: 10.1128/iai.60.8.3369-3375.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Jagusztyn-Krynicka E. K., Smorawinska M., Curtiss R., 3rd Expression of Streptococcus mutans aspartate-semialdehyde dehydrogenase gene cloned into plasmid pBR322. J Gen Microbiol. 1982 May;128(5):1135–1145. doi: 10.1099/00221287-128-5-1135. [DOI] [PubMed] [Google Scholar]
  17. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  20. Lee L. J., Hansen J. B., Jagusztyn-Krynicka E. K., Chassy B. M. Cloning and expression of the beta-D-phosphogalactoside galactohydrolase gene of Lactobacillus casei in Escherichia coli K-12. J Bacteriol. 1982 Dec;152(3):1138–1146. doi: 10.1128/jb.152.3.1138-1146.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lengeler J. Analysis of mutations affecting the dissmilation of galactitol (dulcitol) in Escherichia coli K 12. Mol Gen Genet. 1977 Mar 28;152(1):83–91. doi: 10.1007/BF00264944. [DOI] [PubMed] [Google Scholar]
  22. Maeda S., Gasson M. J. Cloning, expression and location of the Streptococcus lactis gene for phospho-beta-D-galactosidase. J Gen Microbiol. 1986 Feb;132(2):331–340. doi: 10.1099/00221287-132-2-331. [DOI] [PubMed] [Google Scholar]
  23. Oskouian B., Stewart G. C. Cloning and characterization of the repressor gene of the Staphylococcus aureus lactose operon. J Bacteriol. 1987 Dec;169(12):5459–5465. doi: 10.1128/jb.169.12.5459-5465.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Oskouian B., Stewart G. C. Repression and catabolite repression of the lactose operon of Staphylococcus aureus. J Bacteriol. 1990 Jul;172(7):3804–3812. doi: 10.1128/jb.172.7.3804-3812.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Pike L. J., Eakes A. T. Epidermal growth factor stimulates the production of phosphatidylinositol monophosphate and the breakdown of polyphosphoinositides in A431 cells. J Biol Chem. 1987 Feb 5;262(4):1644–1651. [PubMed] [Google Scholar]
  26. Rosey E. L., Stewart G. C. Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans. J Bacteriol. 1992 Oct;174(19):6159–6170. doi: 10.1128/jb.174.19.6159-6170.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Rosey E. L., Stewart G. C. The nucleotide sequence of the lacC and lacD genes of Staphylococcus aureus. Nucleic Acids Res. 1989 May 25;17(10):3980–3980. doi: 10.1093/nar/17.10.3980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Rothstein S. J., Jorgensen R. A., Postle K., Reznikoff W. S. The inverted repeats of Tn5 are functionally different. Cell. 1980 Mar;19(3):795–805. doi: 10.1016/s0092-8674(80)80055-9. [DOI] [PubMed] [Google Scholar]
  29. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  30. Smorawinska M., Hsu J. C., Hansen J. B., Jagusztyn-Krynicka E. K., Abiko Y., Curtiss R., 3rd Clustered genes for galactose metabolism from Streptococcus mutans cloned in Escherichia coli. J Bacteriol. 1983 Feb;153(2):1095–1097. doi: 10.1128/jb.153.2.1095-1097.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Stüber D., Bujard H. Organization of transcriptional signals in plasmids pBR322 and pACYC184. Proc Natl Acad Sci U S A. 1981 Jan;78(1):167–171. doi: 10.1073/pnas.78.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. de Vos W. M., Boerrigter I., van Rooyen R. J., Reiche B., Hengstenberg W. Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis. J Biol Chem. 1990 Dec 25;265(36):22554–22560. [PubMed] [Google Scholar]
  33. van Rooijen R. J., van Schalkwijk S., de Vos W. M. Molecular cloning, characterization, and nucleotide sequence of the tagatose 6-phosphate pathway gene cluster of the lactose operon of Lactococcus lactis. J Biol Chem. 1991 Apr 15;266(11):7176–7181. [PubMed] [Google Scholar]

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

RESOURCES