1887

Abstract

Summary: Previous work has shown that K 12 ColE2 cells undergo a form of partial lysisand exhibit increases in lysophosphatidylethanolamine (lysoPE) and free fatty acid content due to activation of phospholipase A when induced to produce and release colicin E2. The increase in lysoPE content was assumed to be essential for efficientcolicin release. These same characteristics are also presented by some natural ColE2 isolates, and by other representatives of the after transformation with derivatives of a ColE2 plasmid. However, strains carrying ColE2 plasmids released colicin without partial lysis and without increasing their lysoPEcontent. A previously undetected minor phospholipid, which appeared in these and other strains only when they were induced to produce colicin, may be an important factor in colicin release. In ColE2 K 12, production of this new lipid was dependent on phospholipase A activation following expression of the ColE2 lysis gene. Some other ColE2 strains did not respond to induction of colicin production in the same way as ColE2 K 12. These strains were less sensitive to inducer (mitomycin C) or unable to produce increased amounts of colicin in response to induction, or unable to degrade colicin once it was released. In general, the results suggest that colicin release occurs by the same or similar processes in the various strains tested, and support the continued use of K 12 as the model strain for studying the mechanisms of colicin release.

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1985-10-01
2024-12-07
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References

  1. Ames G. F. 1968; Lipids of Salmonella typhimurium and Escherichia coli: structure and metabolism. Journal of Baueriology 95:833–843
    [Google Scholar]
  2. Baker T. A., Howe M. M., Gross C. A. 1984; Mu dX, a derivative of Mu dl(lac ApR) which makes stahie lacZ fusions at high temperalure. Journal of Bactaiology 156:970–974
    [Google Scholar]
  3. Cole S. T., Saint-Joanis B., Pugsley A. P. 1985; Molecular characterization of the colicin E2 operon and identification of its products. Molecular and General Genetics 198:465–472
    [Google Scholar]
  4. De Geus P., Van Die H., Bergmans J., Tommassen J., De Haas G. 1983; Molecular cloning of pldA, the structural gene for outer membrane phospholipase of E. coli K 12. Molecular and General Genetics 190:150–155
    [Google Scholar]
  5. Hancock R. E. W. 1984; Alterations in outer membrane permeability. Annual Review of Microbiology 38:237–264
    [Google Scholar]
  6. Hardaway K. L., Buller C. S. 1979; Effect of ethylenediaminetetraacetic acid on phospholipids and outer membrane function in Escherichia coli. Journal of Bac1erio!ogy 137:62–68
    [Google Scholar]
  7. Henrich B., Lubitz W., Plapp R. 1983; Expression of ϕX174 lysis gene cloned in different plasmids. In The Target of Penicillin pp. 197–203 Edited by Hakenbeck R., Höltje J. V., Labischinski H. Berlin: de Gruyter:
    [Google Scholar]
  8. Holmes D. D., Quigley I. 1981; A rapid boiling method for the preparation of bacterial plasmids. Analytical Biochemistry 114:193–197
    [Google Scholar]
  9. Lugtenberg B., Vanalphen w. 1983; Molecular architecture and functioning of the outer membrane of Escherichia coli and other Gram-negative bacteria. Biochimica et hiophysica acta 737:51–115
    [Google Scholar]
  10. Maniatis T., Fritsch E. F., Sambrook J. 1982 Molecular Cloning, a Laboratory Manual Cold Spring Harbor NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  11. Miller J. H. 1972 c·xperiments in Molernlar Genetics Cold Spring Harbor NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  12. Ohki M., Doi O., Nojima S. 1972; Mutant of Escherichia coli K-12 deficient for detergent-resistant phospholipase A. Journal of Bacteriolog_1 110:864–869
    [Google Scholar]
  13. Oudega B., Stegehuis F., De Graaff K. 1983; Effect of glucose fermentation on the functioning of protein H, involved in excretion of cloacin DF l3. FEMS Microbiology Letters 22:101–108
    [Google Scholar]
  14. Pugsley A. P. 1983a; Colicin E4-CT9 is proteolytically degraded after discharge from producing cells in liquid cultures. Journal of General Microbiologv 129:833–840
    [Google Scholar]
  15. Pugsley A. P. 1983b; Obligatory coupling of colicin release and lysis in mitomycin-treated Col+ Escheri-chia coli. Journal ofGeneral Microbiology 129:1921–1928
    [Google Scholar]
  16. Pugsley A. P. 1984a; The ins and outs of colicins. Part 1. Production and translocation across membranes. Microbiological Sciences 1:168–175
    [Google Scholar]
  17. Pugsley A. P. 1984b; Genetic analysis of ColN plasmid determinants for colicin production, immunity and release. Journal of Bacteriology 158:523–529
    [Google Scholar]
  18. Pugsley A. P. 1985; Escherichia coli K 12 strains for use in the identification and characterization of colicins. Journal of General Microbiologyr 131:369–376
    [Google Scholar]
  19. Pugsley A. P., Rosenbusch J. P. 1981; Release of colicin E2 from Escherichia coli. Journal of Bacteriology 147:186–192
    [Google Scholar]
  20. Pugsley A. P., Schwartz M. 1983a; A genetic approach to the study of mitomycin-induced lysis of Escherichia coli strains which produce colicin E2. Molecular and General Genetics 190:366–372
    [Google Scholar]
  21. Pugsley A. P., Schwartz M. 1983b; Expression of a gene in a 400 base pair fragment of colicin plasmid ColE:2-P9 is sufhcient to cause host cell lysis. Journal of Bacteriology 156:109–114
    [Google Scholar]
  22. Pugsley A. P., Schwartz M. 1984; Colicin E2 release: lysis, leakage or secretion? Possible role of a phospholipase. EMBO Journal 3:2393–2397
    [Google Scholar]
  23. Pugsley A. P., Schwartz M. 1985; Export and secretion of proteins by bacteria. FEMS Microbiology Reriews 1:3–38
    [Google Scholar]
  24. Raetz C. R. H. 1978; Enzymology, genetics and regulation of membrane phospholipid hiosynthesis in Escherichia coli. Microbiological Reviews 42:614–659
    [Google Scholar]
  25. Raibaud O., Mock M., Schwartz M. 1984; A technique for integrating any DNA fragment into the chromosome of Escherichia coli. Gene 29:231–241
    [Google Scholar]
  26. Sakakibara Y., Doi O., Nojima S. 1972; Growth of bacteriophage lambda in phosphohpase A-less mutants. Biochemical and Biophysical Research Communications 46:1434–1440
    [Google Scholar]
  27. Silhavy T. J., Berman M. L., Enqust L. W. 1984 Experiments with Gene Fusivm Cold Spring Harbor NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  28. Skipski V. P., Barclay M. 1969; Thin layer chromatography of lipids. Methods in Enzymology 14:530–598
    [Google Scholar]
  29. Watson R., Konasarka·Kozlowska M., Iyer V. N., Yaguchi M., Vinsenti L. P. 1983; Comparison of plasmids ColE2-P9 and ColE2-CA42 and their immunity proteins. Journal Bacteriology 153:1552–1557
    [Google Scholar]
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