Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1978 Dec;136(3):1070–1083. doi: 10.1128/jb.136.3.1070-1083.1978

A second transport system for sn-glycerol-3-phosphate in Escherichia coli.

M Argast, D Ludtke, T J Silhavy, W Boos
PMCID: PMC218543  PMID: 363686

Abstract

Strains containing phage Mucts inserted into glpT were isolated as fosfomycin-resistant clones. These mutants did not transport sn-glycerol-3-phosphate, and they lacked GLPT, a protein previously shown to be a product of the glpT operon. By plating these mutants on sn-glycerol-3-phosphate at 43 degrees C, we isolated revertants that regained the capacity to grow on G3P. Most of these revertants did not map in glpT and did not regain GLPT. These revertants exhibited a highly efficient uptake system for sn-glycerol-3-phosphate within an apparent Km of 5 micron. In addition, three new proteins (GP 1, 2, and 3) appeared in the periplasm of these revertants. None of these proteins were antigentically related to GLPT. However, like GLPT, GP1 exhibits abnormal behavior on sodium dodecyl sulfate-polyacrylamide gels. GP 2 is an efficient binding protein. The new uptake system showed different characteristics than the system that is coded for by the glpT operon. It was inhibited neither by phosphate nor fosfomycin. So far, none of the systems that transport organic acids in Escherichia coli could be implicated in the new sn-glycerol-3-phosphate uptake activity. The mutation ugp+, which was responsible for the appearance of the new transport system and the appearance of GP 1, 2, and 3 in the periplasm was cotransducible with araD by phage P1 transduction and was recessive in merodiploids.

Full text

PDF
1082

Images in this article

1073Image
on p.1073
1074Image
on p.1074
1076Image
on p.1076
1078Image
on p.1078
1079Image
on p.1079

Selected References

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

  1. Argast M., Schumacher G., Boos W. Characterization of a periplasmic protein related to sn-glycerol-3-phosphate transport in escherichia coli. J Supramol Struct. 1977;6(1):135–153. doi: 10.1002/jss.400060111. [DOI] [PubMed] [Google Scholar]
  2. Boos W., Hartig-Beecken I., Altendorf K. Purification and properties of a periplasmic protein related to sn-glycerol-3-phosphate transport in Escherichia coli. Eur J Biochem. 1977 Feb;72(3):571–581. doi: 10.1111/j.1432-1033.1977.tb11280.x. [DOI] [PubMed] [Google Scholar]
  3. Bukhari A. I. Bacteriophage mu as a transposition element. Annu Rev Genet. 1976;10:389–412. doi: 10.1146/annurev.ge.10.120176.002133. [DOI] [PubMed] [Google Scholar]
  4. Cardelli J., Konisky J. Isolation and characterization of an Escherichia coli mutant tolerant to colicins Ia and Ib. J Bacteriol. 1974 Aug;119(2):379–385. doi: 10.1128/jb.119.2.379-385.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cozzarelli N. R., Freedberg W. B., Lin E. C. Genetic control of L-alpha-glycerophosphate system in Escherichia coli. J Mol Biol. 1968 Feb 14;31(3):371–387. doi: 10.1016/0022-2836(68)90415-4. [DOI] [PubMed] [Google Scholar]
  6. Epstein W., Kim B. S. Potassium transport loci in Escherichia coli K-12. J Bacteriol. 1971 Nov;108(2):639–644. doi: 10.1128/jb.108.2.639-644.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Freedberg W. B., Lin E. C. Three kinds of controls affecting the expression of the glp regulon in Escherichia coli. J Bacteriol. 1973 Sep;115(3):816–823. doi: 10.1128/jb.115.3.816-823.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. GAREN A., LEVINTHAL C. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase. Biochim Biophys Acta. 1960 Mar 11;38:470–483. doi: 10.1016/0006-3002(60)91282-8. [DOI] [PubMed] [Google Scholar]
  9. Guardiola J., De Felice M., Klopotowski T., Iaccarino M. Mutations affecting the different transport systems for isoleucine, leucine, and valine in Escherichia coli K-12. J Bacteriol. 1974 Feb;117(2):393–405. doi: 10.1128/jb.117.2.393-405.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. HAYASHI S., KOCH J. P., LIN E. C. ACTIVE TRANSPORT OF L-ALPHA-GLYCEROPHOSPHATE IN ESCHERICHIA COLI. J Biol Chem. 1964 Sep;239:3098–3105. [PubMed] [Google Scholar]
  11. Hacking A. J., Lin E. C. Regulatory changes in the fucose system associated with the evolution of a catabolic pathway for propanediol in Escherichia coli. J Bacteriol. 1977 May;130(2):832–838. doi: 10.1128/jb.130.2.832-838.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Howe M. M., Bade E. G. Molecular biology of bacteriophage mu. Science. 1975 Nov 14;190(4215):624–632. doi: 10.1126/science.1103291. [DOI] [PubMed] [Google Scholar]
  13. Johnson W. C., Silhavy T. J., Boos W. Two-dimensional polyacylamide gel electrophoresis of envelope proteins of Escherichia coli. Appl Microbiol. 1975 Mar;29(3):405–413. doi: 10.1128/am.29.3.405-413.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kistler W. S., Lin E. C. Anaerobic L- -glycerophosphate dehydrogenase of Escherichia coli: its genetic locus and its physiological role. J Bacteriol. 1971 Dec;108(3):1224–1234. doi: 10.1128/jb.108.3.1224-1234.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  16. Lagarde A. E., Pouysségur J. M., Stoeber F. R. A transport system for 2-keto-3-deoxy-D-gluconate uptake in Escherichia coli K12. Biochemical and physiological studies in whole cells. Eur J Biochem. 1973 Jul 16;36(2):328–341. doi: 10.1111/j.1432-1033.1973.tb02917.x. [DOI] [PubMed] [Google Scholar]
  17. Lin E. C. Glycerol dissimilation and its regulation in bacteria. Annu Rev Microbiol. 1976;30:535–578. doi: 10.1146/annurev.mi.30.100176.002535. [DOI] [PubMed] [Google Scholar]
  18. Ljungquist E., Bukhari A. I. State of prophage Mu DNA upon induction. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3143–3147. doi: 10.1073/pnas.74.8.3143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Messer A. Lactose permeation via the arabinose transport system in Escherichia coli K-12. J Bacteriol. 1974 Oct;120(1):266–272. doi: 10.1128/jb.120.1.266-272.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Neu H. C., Heppel L. A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem. 1965 Sep;240(9):3685–3692. [PubMed] [Google Scholar]
  21. Reeve J. N., Groves D. J., Clark D. J. Regulation of Cell Division in Escherichia coli: Characterization of Temperature-Sensitive Division Mutants. J Bacteriol. 1970 Dec;104(3):1052–1064. doi: 10.1128/jb.104.3.1052-1064.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Reiner A. M. Xylitol and D-arabitol toxicities due to derepressed fructose, galactitol, and sorbitol phosphotransferases of Escherichia coli. J Bacteriol. 1977 Oct;132(1):166–173. doi: 10.1128/jb.132.1.166-173.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Saier M. H., Jr Bacterial phosphoenolpyruvate: sugar phosphotransferase systems: structural, functional, and evolutionary interrelationships. Bacteriol Rev. 1977 Dec;41(4):856–871. doi: 10.1128/br.41.4.856-871.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Schumacher G., Bussmann K. Cell-free synthesis of proteins related to sn-glycerol-3-phosphate transport in Escherichia coli. J Bacteriol. 1978 Jul;135(1):239–250. doi: 10.1128/jb.135.1.239-250.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Shen B. H., Boos W. Regulation of the -methylgalactoside transport system and the galatose-binding protein by the cell cycle of Escherichia coli. Proc Natl Acad Sci U S A. 1973 May;70(5):1481–1485. doi: 10.1073/pnas.70.5.1481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Silhavy T. J., Casadaban M. J., Shuman H. A., Beckwith J. R. Conversion of beta-galactosidase to a membrane-bound state by gene fusion. Proc Natl Acad Sci U S A. 1976 Oct;73(10):3423–3427. doi: 10.1073/pnas.73.10.3423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Silhavy T. J., Hartig-Beecken I., Boos W. Periplasmic protein related to the sn-glycerol-3-phosphate transport system of Escherichia coli. J Bacteriol. 1976 May;126(2):951–958. doi: 10.1128/jb.126.2.951-958.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Venkateswaran P. S., Wu H. C. Isolation and characterization of a phosphonomycin-resistant mutant of Escherichia coli K-12. J Bacteriol. 1972 Jun;110(3):935–944. doi: 10.1128/jb.110.3.935-944.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES