1887

Abstract

SUMMARY: The killing of a population of a sensitive strain of by halocin H4 followed exponential kinetics, and the percentage survival of sensitive cells exposed to different concentrations of halocin H4 corresponded to single-hit-type kinetics. Morphological changes were observed in treated cells, which showed swollen, spherical shapes. Halocin H4 affected macromolecule synthesis very little, and only late after the start of the treatment, although the transport of 2-aminoisobutyric acid, a non-metabolizable amino acid, was rapidly stopped. Bacteriorhodopsin-mediated H extrusion worked very efficiently in treated cells, and much larger pH decreases were found in treated than in untreated suspensions after illumination, although ATP synthesis was not markedly affected. These findings suggest that the primary target of halocin H4 may be located in the membrane, producing permeability changes and ionic imbalance, which lead to death and cell lysis.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-132-11-3061
1986-11-01
2021-10-25
Loading full text...

Full text loading...

/deliver/fulltext/micro/132/11/mic-132-11-3061.html?itemId=/content/journal/micro/10.1099/00221287-132-11-3061&mimeType=html&fmt=ahah

References

  1. Danon A., Stoeckenius W. 1974; Photophosphorylation in Halobacterium halobium. Proceedings of the National Academy of Sciences of the United States of America 71:1234–1238
    [Google Scholar]
  2. Hirsch H. J., Tsai H., Geffers I. 1978; Purification and effects of fulvocin C, a bacteriocin from Myxococcus fulvus Mxf16. Archives of Microbiology 119:279–286
    [Google Scholar]
  3. Hubbard J. S., Rinehart C. A., Baker R. A. 1976; Energy coupling in the active transport of amino acids by bacteriorhodopsin-containing cells of Halobacterium halobium. Journal of Bacteriology 125:181–190
    [Google Scholar]
  4. Juez G., Rodriguez-Valera F. 1984; A mutant of Halobacterium halobium with constitutive production of bacteriorhodopsin. FEMS Microbiology Letters 23:167–170
    [Google Scholar]
  5. Konisky J. 1982; Colicins and other bacteriocins with established modes of action. Annual Review of Microbiology 36:125–144
    [Google Scholar]
  6. Krulwich T. A. 1983; Na+/H+ antiporters. Biochimica et biophysica acta 726:245–264
    [Google Scholar]
  7. Levisohn R., Konisky J., Nomura M. 1967; Interaction of colicins with bacterial cells. IV. Immunity breakdown studied with colicins la and lb. Journal of Bacteriology 96:811–821
    [Google Scholar]
  8. Mescher M. F., Strominger J. L. 1978; The cell surface glycoprotein of Halobacterium salinarium. In Energetics and Structure of Halophilic Micro-organisms pp. 503–514 Edited by Kaplan S. R., Ginzburg H. Amsterdam New York: Elsevier/ North Holland Biomedical Press;
    [Google Scholar]
  9. Meseguer I., Rodriguez-Valera F. 1985; Production and purification of halocin H4. FEMS Microbiology Letters 28:177–182
    [Google Scholar]
  10. Ozaki M., Higashi Y., Saito H., An T., Amano T. 1966; Identity of megacin A with phospholipase A. Biken Journal 9:201–213
    [Google Scholar]
  11. Reeves P. 1965; The bacteriocins. Bacteriological Reviews 29:24–45
    [Google Scholar]
  12. Rodriguez-Valera F., Juez G., Kushner D. J. 1982; Halocins: salt-dependent bacteriocins produced by extremely halophilic rods. Canadian Journal of Microbiology 28:151–154
    [Google Scholar]
  13. Rodriguez-Valera F., Juez G., Kushner D. J. 1983; Halobacterium mediterranei spec, nov., a new carbohydrate-utilizing extreme halophile. Systematic and Applied Microbiology 4:369–381
    [Google Scholar]
  14. Sahl H. G., Brandis H. 1982; Mode of action of the staphylococcin-like peptide Pep-5 and culture conditions affecting its activity. Zentralblatt fur Bakteriologie und Hygiene (Abteilung originate A) 252:166–175
    [Google Scholar]
  15. Schaller K., Höltje J. V., Braun V. 1982; Colicin M is an inhibitor of murein biosynthesis. Journal of Bacteriology 152:994–1000
    [Google Scholar]
  16. Stoeckenius W., Rowen R. 1967; A morphological study of Halobacterium halobium and its lysis in media of low salt concentrations. Journal of Cell Biology 34:365–393
    [Google Scholar]
  17. Tagg J. R., Dajani A. S., Wannamaker L. W. 1976; Bacteriocins of Gram-positive bacteria. Bacteriological Reviews 40:722–756
    [Google Scholar]
  18. Timmis K. 1972; Purification and characterization of colicin D. Journal of Bacteriology 109:19–20
    [Google Scholar]
  19. Woese C. R., Fox G. E. 1977; Phylogenetic structure of the prokaryotic domain: the primary kingdoms. Proceedings of the National Academy of Sciences of the United States of America 74:5088–5090
    [Google Scholar]
  20. Yang C. C., Konisky J. 1984; Colicin V-treated Escherichia coli does not generate membrane poten tial. Journal of Bacteriology 158:757–759
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-132-11-3061
Loading
/content/journal/micro/10.1099/00221287-132-11-3061
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error