Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1976 Mar;125(3):910–915. doi: 10.1128/jb.125.3.910-915.1976

Diminution of outer membrane permeability by Mg2+ in a marine pseudomonad.

H Moustafa Hassan
PMCID: PMC236166  PMID: 1254558

Abstract

Intact cells of the marine pseudomonad MB-45, in the presence of optimal Mg2+, exhibited little alkaline phosphatase activity as judged by the hydrolysis of p-nitrophenylphosphate. Sonic extracts, in contrast, were rich in this activity. Removal of the loosely bound outer layer did not diminish this crypticity of alkaline phosphatase, but decreasing the concentration of Mg2+ in the suspending medium progressively exposed the alkaline phosphatase. Since MB-45 did not liberate alkaline phosphatase into the surrounding medium even in the absence of Mg2+ and since this enzyme is localized in the periplasmic space, it can be concluded that the crypticity was due to the exclusion of p-nitrophenylphosphate by the outer membrane. Mg2+ is apparently essential for the full expression of this limited permeability.

Full text

PDF
910

Selected References

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

  1. Beacham I. R., Kahana R., Levy L., Yagil E. Mutants of Escherichia coli K-12 "cryptic," or deficient in 5'-nucleotidase (uridine diphosphate-sugar hydrolase) and 3'-nucleotidase (cyclic phosphodiesterase) activity. J Bacteriol. 1973 Nov;116(2):957–964. doi: 10.1128/jb.116.2.957-964.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brockman R. W., Heppel L. A. On the localization of alkaline phosphatase and cyclic phosphodiesterase in Escherichia coli. Biochemistry. 1968 Jul;7(7):2554–2562. doi: 10.1021/bi00847a016. [DOI] [PubMed] [Google Scholar]
  3. Buckmire F. L., MacLeod R. A. Evidence for the release at low salt concentration of a lipid-protein-carbohydrate complex from isolated envelopes and whole cells of a marine pseudomonad. Can J Microbiol. 1971 May;17(5):713–723. doi: 10.1139/m71-114. [DOI] [PubMed] [Google Scholar]
  4. Cheng J. K., Costerton J. W., Singh A. P., Ingram J. M. Susceptibility of whole cells and spheroplasts of Pseudomonas aeruginosa to actinomycin D. Antimicrob Agents Chemother. 1973 Mar;3(3):399–406. doi: 10.1128/aac.3.3.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Costerton J. W., Ingram J. M., Cheng K. J. Structure and function of the cell envelope of gram-negative bacteria. Bacteriol Rev. 1974 Mar;38(1):87–110. doi: 10.1128/br.38.1.87-110.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. De Voe I. W., Oginsky E. L. Antagonistic effect of monovalent cations in maintenance of cellular integrity of a marine bacterium. J Bacteriol. 1969 Jun;98(3):1355–1367. doi: 10.1128/jb.98.3.1355-1367.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eagon R. G., Simmons G. P., Carson K. J. Evidence for the presence of ash and fivalent metals in the cell wall of Pseudomonas aeruginosa. Can J Microbiol. 1965 Dec;11(6):1041–1042. doi: 10.1139/m65-144. [DOI] [PubMed] [Google Scholar]
  8. Forsberg C. W., Costerton J. W., Macleod R. A. Separation and localization of cell wall layers of a gram-negative bacterium. J Bacteriol. 1970 Dec;104(3):1338–1353. doi: 10.1128/jb.104.3.1338-1353.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gustafsson P., Nordström K., Normark S. Outer penetration barrier of Escherichia coli K-12: kinetics of the uptake of gentian violet by wild type and envelope mutants. J Bacteriol. 1973 Nov;116(2):893–900. doi: 10.1128/jb.116.2.893-900.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Inouye M. A three-dimensional molecular assembly model of a lipoprotein from the Escherichia coli outer membrane. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2396–2400. doi: 10.1073/pnas.71.6.2396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MacAlister T. J., Costerton J. W., Cheng K. J. Effect of the removal of outer cell wall layers on the actinomycin susceptibility of a gram-negative bacterium. Antimicrob Agents Chemother. 1972 May;1(5):447–449. doi: 10.1128/aac.1.5.447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McQUILLEN K. Lysis resulting from metabolic disturbance. J Gen Microbiol. 1958 Apr;18(2):498–512. doi: 10.1099/00221287-18-2-498. [DOI] [PubMed] [Google Scholar]
  13. Nakae T. Outer membrane of Salmonella typhimurium: reconstitution of sucrose-permeable membrane vesicles. Biochem Biophys Res Commun. 1975 Jun 16;64(4):1224–1230. doi: 10.1016/0006-291x(75)90823-2. [DOI] [PubMed] [Google Scholar]
  14. Scherrer R., Gerhardt P. Influence of magnesium ions on porosity of the Bacillus megaterium cell wall and membrane. J Bacteriol. 1973 May;114(2):888–890. doi: 10.1128/jb.114.2.888-890.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. TYLER M. E., BIELLING M. C., PRATT D. B. Mineral requirements and other characters of selected marine bacteria. J Gen Microbiol. 1960 Aug;23:153–161. doi: 10.1099/00221287-23-1-153. [DOI] [PubMed] [Google Scholar]
  16. Thompson L. M., MacLeod R. A. Biochemical localization of alkaline phosphatase in the cell wall of a marine pseudomonad. J Bacteriol. 1974 Feb;117(2):819–825. doi: 10.1128/jb.117.2.819-825.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Unemoto T., MacLeod R. A. Capacity of the outer membrane of a gram-negative marine bacterium in the presence of cations to prevent lysis by Triton X-100. J Bacteriol. 1975 Mar;121(3):800–806. doi: 10.1128/jb.121.3.800-806.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES