Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1973 May;114(2):723–728. doi: 10.1128/jb.114.2.723-728.1973

Membrane Translocation of Mannitol in Escherichia coli Without Phosphorylation

Ellen Solomon a,1, Kenji Miyai a,2, E C C Lin a
PMCID: PMC251832  PMID: 4574698

Abstract

Galactosyl-mannitol can be transported into cells of Escherichia coli by β-galactoside permease and can be hydrolyzed rapidly to mannitol and galactose by β-galactosidase. When a mutant strain lacking enzyme I of the phosphoenolpyruvate phosphotransferase system and constitutive in the lactose system was presented with galactosyl-mannitol in which the mannitol moiety was labeled with 3H, the liberated mannitol remained inside the cell if the Enzyme II complex of the phosphoenolpyruvate phosphotransferase system for mannitol was uninduced. It is postualted that one of the enzyme II proteins can still catalyze translocation of mannitol across the cell membrane even when phsophorylation is not possible.

Full text

PDF
726

Selected References

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

  1. ASENSIO C., AVIGAD G., HORECKER B. L. PREFERENTIAL GALACTOSE UTILIZATION IN A MUTANT STRAIN OF E. COLI. Arch Biochem Biophys. 1963 Dec;103:299–309. doi: 10.1016/0003-9861(63)90419-3. [DOI] [PubMed] [Google Scholar]
  2. Adhya S., Echols H. Glucose effect and the galactose enzymes of Escherichia coli: correlation between glucose inhibition of induction and inducer transport. J Bacteriol. 1966 Sep;92(3):601–608. doi: 10.1128/jb.92.3.601-608.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Anderson B., Weigel N., Kundig W., Roseman S. Sugar transport. 3. Purification and properties of a phosphocarrier protein (HPr) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. J Biol Chem. 1971 Nov 25;246(22):7023–7033. [PubMed] [Google Scholar]
  4. Anraku Y. Transport of sugars and amino acids in bacteria. I. Purification and specificity of the galactose- and leucine-binding proteins. J Biol Chem. 1968 Jun 10;243(11):3116–3122. [PubMed] [Google Scholar]
  5. Berman M., Lin E. C. Glycerol-specific revertants of a phosphoenolpyruvate phosphotransferase mutant: suppression by the desensitization of glycerol kinase to feedback inhibition. J Bacteriol. 1971 Jan;105(1):113–120. doi: 10.1128/jb.105.1.113-120.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Boos W., Lengeler J., Hermann K. O., Unsöld H. J. The regulation of the beta-methylgalactoside transport system and of the galactose binding protein of Escherichia coli K12. Eur J Biochem. 1971 Apr 30;19(4):457–470. doi: 10.1111/j.1432-1033.1971.tb01336.x. [DOI] [PubMed] [Google Scholar]
  7. Boos W. The galactose binding protein and its relationship to the beta-methylgalactoside permease from Escherichia coli. Eur J Biochem. 1969 Aug;10(1):66–73. doi: 10.1111/j.1432-1033.1969.tb00656.x. [DOI] [PubMed] [Google Scholar]
  8. FRAENKEL D. G., FALCOZ-KELLY F., HORECKER B. L. THE UTILIZATION OF GLUCOSE 6-PHOSPHATE BY GLUCOKINASELESS AND WILD-TYPE STRAINS OF ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1964 Nov;52:1207–1213. doi: 10.1073/pnas.52.5.1207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. 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]
  11. Kamogawa A., Kurahashi K. Inhibitory effect of glucose on the growth of a mutant strain of Escherichia coli defective in glucose transport system. J Biochem. 1967 Feb;61(2):220–230. doi: 10.1093/oxfordjournals.jbchem.a128534. [DOI] [PubMed] [Google Scholar]
  12. Kundig W., Roseman S. Sugar transport. I. Isolation of a phosphotransferase system from Escherichia coli. J Biol Chem. 1971 Mar 10;246(5):1393–1406. [PubMed] [Google Scholar]
  13. Kundig W., Roseman S. Sugar transport. II. Characterization of constitutive membrane-bound enzymes II of the Escherichia coli phosphotransferase system. J Biol Chem. 1971 Mar 10;246(5):1407–1418. [PubMed] [Google Scholar]
  14. Lin E. C. The genetics of bacterial transport systems. Annu Rev Genet. 1970;4:225–262. doi: 10.1146/annurev.ge.04.120170.001301. [DOI] [PubMed] [Google Scholar]
  15. PARDEE A. B., PRESTIDGE L. S. The initial kinetics of enzyme induction. Biochim Biophys Acta. 1961 Apr 29;49:77–88. doi: 10.1016/0006-3002(61)90871-x. [DOI] [PubMed] [Google Scholar]
  16. Pastan I., Perlman R. L. Repression of beta-galactosidase synthesis by glucose in phosphotransferase mutants of Escherichia coli. Repression in the absence of glucose phosphorylation. J Biol Chem. 1969 Nov 10;244(21):5836–5842. [PubMed] [Google Scholar]
  17. Romano A. H., Eberhard S. J., Dingle S. L., McDowell T. D. Distribution of the phosphoenolpyruvate: glucose phosphotransferase system in bacteria. J Bacteriol. 1970 Nov;104(2):808–813. doi: 10.1128/jb.104.2.808-813.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sanno Y., Wilson T. H., Lin E. C. Control of permeation to glycerol in cells of Escherichia coli. Biochem Biophys Res Commun. 1968 Jul 26;32(2):344–349. doi: 10.1016/0006-291x(68)90392-6. [DOI] [PubMed] [Google Scholar]
  19. Simoni R. D., Levinthal M., Kundig F. D., Kundig W., Anderson B., Hartman P. E., Roseman S. Genetic evidence for the role of a bacterial phosphotransferase system in sugar transport. Proc Natl Acad Sci U S A. 1967 Nov;58(5):1963–1970. doi: 10.1073/pnas.58.5.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Solomon E., Lin E. C. Mutations affecting the dissimilation of mannitol by Escherichia coli K-12. J Bacteriol. 1972 Aug;111(2):566–574. doi: 10.1128/jb.111.2.566-574.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Solomon E., Miyai K., Jeanloz R. W. Synthesis and use of 1-O- -D-galactopyranosyl-D-mannitol as source of D-mannitol for Escherichia coli. Biochemistry. 1971 May 11;10(10):1803–1807. doi: 10.1021/bi00786a011. [DOI] [PubMed] [Google Scholar]
  22. Tanaka S., Fraenkel D. G., Lin E. C. The enzymatic lesion of strain MM-6, a pleiotropic carbohydrate-negative mutant of Escherichia coli. Biochem Biophys Res Commun. 1967 Apr 7;27(1):63–67. doi: 10.1016/s0006-291x(67)80040-8. [DOI] [PubMed] [Google Scholar]
  23. Tanaka S., Lerner S. A., Lin E. C. Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol. J Bacteriol. 1967 Feb;93(2):642–648. doi: 10.1128/jb.93.2.642-648.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. 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