Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1977 Aug;131(2):505–511. doi: 10.1128/jb.131.2.505-511.1977

Two systems for the uptake of phosphate in Escherichia coli.

H Rosenberg, R G Gerdes, K Chegwidden
PMCID: PMC235458  PMID: 328484

Abstract

Mutants of Escherichia coli K-12 were constructed such that each possessed one single major system for phosphate transport. A comparison of these strains showed that one of the systems (PIT) was fully constitutive, required no binding protein, and operated in spheroplasts. It permitted the complete exchange of intracellular phosphate with extracellular phosphate (or arsenate) and was completely inhibited by uncouplers. The other system, PST, was repressible by phosphate concentrations above 1 mM, required the phosphate-binding protein for full activity, and did not operate in spheroplasts. It catalyzed very little exchange between internal and external phosphate and was resistant to uncouplers. The maximal velocities attained by the two systems were approximately the same, but the affinity for phosphate in the PST system was greater by two orders of magnitude. In strains in which both systems were fully operative, the initial rates of uptake was nearly additive, and the systems appeared to interact with a common intracellular phosphate pool.

Full text

PDF
505

Selected References

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

  1. Bachmann B. J., Low K. B., Taylor A. L. Recalibrated linkage map of Escherichia coli K-12. Bacteriol Rev. 1976 Mar;40(1):116–167. doi: 10.1128/br.40.1.116-167.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bennett R. L., Malamy M. H. Arsenate resistant mutants of Escherichia coli and phosphate transport. Biochem Biophys Res Commun. 1970 Jul 27;40(2):496–503. doi: 10.1016/0006-291x(70)91036-3. [DOI] [PubMed] [Google Scholar]
  3. Berger E. A., Heppel L. A. Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli. J Biol Chem. 1974 Dec 25;249(24):7747–7755. [PubMed] [Google Scholar]
  4. Blasco F., Ducet G., Azoulay E. Mise en évidence de deux systèmes de transport du phosphate chez Candida tropicalis. Biochimie. 1976;58(3):351–357. doi: 10.1016/s0300-9084(76)80442-7. [DOI] [PubMed] [Google Scholar]
  5. ECHOLS H., GAREN A., GAREN S., TORRIANI A. Genetic control of repression of alkaline phosphatase in E. coli. J Mol Biol. 1961 Aug;3:425–438. doi: 10.1016/s0022-2836(61)80055-7. [DOI] [PubMed] [Google Scholar]
  6. Gerdes R. G., Rosenberg H. The relationship between the phosphate-binding protein and a regulator gene product from Escherichia coli. Biochim Biophys Acta. 1974 May 10;351(1):77–86. doi: 10.1016/0005-2795(74)90066-x. [DOI] [PubMed] [Google Scholar]
  7. Gerdes R. G., Strickland K. P., Rosenberg H. Restoration of phosphate transport by the phosphate-binding protein in spheroplasts of Escherichia coli. J Bacteriol. 1977 Aug;131(2):512–518. doi: 10.1128/jb.131.2.512-518.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Harold F. M., Baarda J. R. Interaction of arsenate with phosphate-transport systems in wild- type and mutant Streptococcus faecalis. J Bacteriol. 1966 Jun;91(6):2257–2262. doi: 10.1128/jb.91.6.2257-2262.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Harold F. M., Spitz E. Accumulation of arsenate, phosphate, and aspartate by Sreptococcus faecalis. J Bacteriol. 1975 Apr;122(1):266–277. doi: 10.1128/jb.122.1.266-277.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kida S. The biological function of the R2a regulatory gene for alkaline phosphatase in Escherichia coli. Arch Biochem Biophys. 1974 Jul;163(1):231–237. doi: 10.1016/0003-9861(74)90473-1. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. MITCHELL P. Transport of phosphate across the osmotic barrier of Micrococcus pyogenes; specificity and kinetics. J Gen Microbiol. 1954 Aug;11(1):73–82. doi: 10.1099/00221287-11-1-73. [DOI] [PubMed] [Google Scholar]
  13. Medveczky N., Rosenberg H. Phosphate transport in Escherichia coli. Biochim Biophys Acta. 1971 Aug 13;241(2):494–506. doi: 10.1016/0005-2736(71)90048-4. [DOI] [PubMed] [Google Scholar]
  14. PITTARD J. EFFECT OF INTEGRATED SEX FACTOR ON TRANSDUCTION OF CHROMOSOMAL GENES IN ESCHERICHIA COLI. J Bacteriol. 1965 Mar;89:680–686. doi: 10.1128/jb.89.3.680-686.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rae A. S., Strickland K. P., Medveczky N., Rosenberg H. Studies of phosphate transport in Escherichia coli. I. Reexamination of the effect of osmotic and cold shock on phosphate uptake and some attempts to restore uptake with phosphate binding protein. Biochim Biophys Acta. 1976 May 21;433(3):555–563. doi: 10.1016/0005-2736(76)90281-9. [DOI] [PubMed] [Google Scholar]
  16. Rae A. S., Strickland K. P. Studies on phosphate transport in Escherichia coli. II. Effects of metabolic inhibitors and divalent cations. Biochim Biophys Acta. 1976 May 21;433(3):564–582. doi: 10.1016/0005-2736(76)90282-0. [DOI] [PubMed] [Google Scholar]
  17. Rosenberg H., Cox G. B., Butlin J. D., Gutowski S. J. Metabolite transport in mutants of Escherichia coli K12 defective in electron transport and coupled phosphorylation. Biochem J. 1975 Feb;146(2):417–423. doi: 10.1042/bj1460417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sprague G. F., Jr, Bell R. M., Cronan J. E., Jr A mutant of Escherichia coli auxotrophic for organic phosphates: evidence for two defects in inorganic phosphate transport. Mol Gen Genet. 1975 Dec 30;143(1):71–77. doi: 10.1007/BF00269422. [DOI] [PubMed] [Google Scholar]
  19. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Willsky G. R., Bennett R. L., Malamy M. H. Inorganic phosphate transport in Escherichia coli: involvement of two genes which play a role in alkaline phosphatase regulation. J Bacteriol. 1973 Feb;113(2):529–539. doi: 10.1128/jb.113.2.529-539.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Willsky G. R., Malamy M. H. Control of the synthesis of alkaline phosphatase and the phosphate-binding protein in Escherichia coli. J Bacteriol. 1976 Jul;127(1):595–609. doi: 10.1128/jb.127.1.595-609.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Willsky G. R., Malamy M. H. The loss of the phoS periplasmic protein leads to a change in the specificity of a constitutive inorganic phosphate transport system in Escherichia coli. Biochem Biophys Res Commun. 1974 Sep 9;60(1):226–233. doi: 10.1016/0006-291x(74)90195-8. [DOI] [PubMed] [Google Scholar]

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

RESOURCES