Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1974 Nov;120(2):866–871. doi: 10.1128/jb.120.2.866-871.1974

Source of Energy for the Escherichia coli Galactose Transport Systems Induced by Galactose

David B Wilson 1
PMCID: PMC245850  PMID: 4281777

Abstract

The β-methyl-galactoside- and galactose-specific transport systems of Escherichia coli were shown by experiments involving inhibitors and the use of an adenosine triphosphatase mutant strain to utilize adenosine 5′-triphosphate or a related compound to drive active transport. These systems were shown to be unable to use the activated-membrane state. The galactose-specific transport system was shown to behave most like a member of the binding-protein class of transport systems by its response to osmotic shock and vesicle formation. These results extended to two sugar transport systems: the correlation between the source of energy and class of transport system found by Berger (1973) for amino acid transport systems. That is, binding-protein systems utilized adenosine 5′-triphosphate whereas membrane-bound systems utilized the activated-membrane state to drive active transport.

Full text

PDF
866

Selected References

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

  1. Ames G. F., Lever J. Components of histidine transport: histidine-binding proteins and hisP protein. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1096–1103. doi: 10.1073/pnas.66.4.1096. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Berger E. A. Different mechanisms of energy coupling for the active transport of proline and glutamine in Escherichia coli. Proc Natl Acad Sci U S A. 1973 May;70(5):1514–1518. doi: 10.1073/pnas.70.5.1514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boos W. Structurally defective galactose-binding protein isolated from a mutant negative in the -methylgalactoside transport system of Escherichia coli. J Biol Chem. 1972 Sep 10;247(17):5414–5424. [PubMed] [Google Scholar]
  4. 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]
  5. Butlin J. D., Cox G. B., Gibson F. Oxidative phosphorylation in Escherichia coli K12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase. Biochem J. 1971 Aug;124(1):75–81. doi: 10.1042/bj1240075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kaback H. R. Transport across isolated bacterial cytoplasmic membranes. Biochim Biophys Acta. 1972 Aug 4;265(3):367–416. doi: 10.1016/0304-4157(72)90014-7. [DOI] [PubMed] [Google Scholar]
  7. Kanner B. I., Gutnick D. L. Energy linked nicotinamide adenine dinucleotide transhydrogenase in a mutant of Escherichia coli K12 lacking membrane Mg(2+)&z.sbnd;Ca(2+)-activated adenosine triphosphatase. FEBS Lett. 1972 May 1;22(2):197–199. doi: 10.1016/0014-5793(72)80043-7. [DOI] [PubMed] [Google Scholar]
  8. Kepes A. Trois classes de systèmes de transport chez les bactéries. Biochimie. 1973;55(6):693–702. [PubMed] [Google Scholar]
  9. Kerwar G. K., Gordon A. S., Kaback H. R. Mechanisms of active transport in isolated membrane vesicles. IV. Galactose transport by isolated membrane vesicles from Escherichia coli. J Biol Chem. 1972 Jan 10;247(1):291–297. [PubMed] [Google Scholar]
  10. Klein W. L., Boyer P. D. Energization of active transport by Escherichia coli. J Biol Chem. 1972 Nov 25;247(22):7257–7265. [PubMed] [Google Scholar]
  11. Konings W. N., Kaback H. R. Anaerobic transport in Escherichia coli membrane vesicles. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3376–3381. doi: 10.1073/pnas.70.12.3376. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Parnes J. R., Boos W. Energy coupling of the -methylgalactoside transport system of Escherichia coli. J Biol Chem. 1973 Jun 25;248(12):4429–4435. [PubMed] [Google Scholar]
  14. Pavlasova E., Harold F. M. Energy coupling in the transport of beta-galactosides by Escherichia coli: effect of proton conductors. J Bacteriol. 1969 Apr;98(1):198–204. doi: 10.1128/jb.98.1.198-204.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rotman B., Ganesan A. K., Guzman R. Transport systems for galactose and galactosides in Escherichia coli. II. Substrate and inducer specificities. J Mol Biol. 1968 Sep 14;36(2):247–260. doi: 10.1016/0022-2836(68)90379-3. [DOI] [PubMed] [Google Scholar]
  16. Schairer H. U., Haddock B. A. -Galactoside accumulation in a Mg 2+ -,Ca 2+ -activated ATPase deficient mutant of E.coli. Biochem Biophys Res Commun. 1972 Aug 7;48(3):544–551. doi: 10.1016/0006-291x(72)90382-8. [DOI] [PubMed] [Google Scholar]
  17. Simoni R. D., Shallenberger M. K. Coupling of energy to active transport of amino acids in Escherichia coli. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2663–2667. doi: 10.1073/pnas.69.9.2663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. 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]
  19. Vorisek J., Kepes A. Galactose transport in Escherichia coli and the galactose-binding protein. Eur J Biochem. 1972 Jul 24;28(3):364–372. doi: 10.1111/j.1432-1033.1972.tb01922.x. [DOI] [PubMed] [Google Scholar]
  20. Wilson D. B. The regulation and properties of the galactose transport system in Escherichia coli K12. J Biol Chem. 1974 Jan 25;249(2):553–558. [PubMed] [Google Scholar]

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

RESOURCES