1887

Abstract

Seven temperature-sensitive penicillin-tolerant mutants of strain LD5 () were isolated and characterized. Treatment with -lactams caused lysis of the mutants at 30 °C. Although growth of the mutants at 42 °C was inhibited by -lactams, no lysis occurred. The mutants were also slightly tolerant to -cycloserine at 42 °C but lysed readily when deprived of diaminopimelate or when treated with moenomycin. The minimum inhibitory concentrations of various antibiotics were the same for the mutants and their parent. The mutations conferring penicillin tolerance were phenotypically suppressed in the presence of a variety of compounds which may act as chaotropic or antichaotropic agents. No defects in penicillin-binding proteins and peptidoglycan hydrolases were detected. Temperature-resistant revertants of the mutants were no longer tolerant to penicillin-induced autolysis at 42 °C. The mutations in five isolates were localized to the 56 to 61 min region of the linkage map and to the 44 to 51 min region in the case of two other isolates.

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/content/journal/micro/10.1099/00221287-130-6-1315
1984-06-01
2024-03-29
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References

  1. Beck B. C., Park J. T. 1976; Activity of three murein hydrolases during the cell division of Escherichia coli K-12 as measured in toluene-treated cells. Journal of Bacteriology 126:1250–1260
    [Google Scholar]
  2. Egan A. F., Russell R. R. B. 1973; Conditional mutations affecting the cell envelope of Escherichia coli K-12. Genetical Research 21:139–152
    [Google Scholar]
  3. Goodell E. W., schwarz U. 1977; Enzymes synthesizing and hydrolysing murein in Escherichia coli. Topographical distribution over the cell envelope. European Journal of Biochemistry 81:205–210
    [Google Scholar]
  4. Hakenbeck R., Goodell E. W., schwarz U. 1974; Compartmentalization of murein hydrolases in the envelope of Escherichia coli. FEBS Letters 40:261–264
    [Google Scholar]
  5. Harkness R. E., Ishiguro E. E. 1983; Temperature-sensitive autolysis-defective mutants of Escherichia coli. Journal of Bacteriology 155:15–21
    [Google Scholar]
  6. Hartmann R., Höltje J. V., schwarz U. 1972; Targets of penicillin action in Escherichia coli. Nature; London: 235426–429
    [Google Scholar]
  7. Hartmann R., Bock-Hennig S. B., schwarz U. 1974; Murein hydrolases in the envelope of Escherichia coli. Properties in situ and solubilization from the envelope. European Journal of Biochemistry 41:203–208
    [Google Scholar]
  8. Hatefi Y., Hanstein W. G. 1974; Destabilization of membranes with chaotropic ions. Methods in Enzymology 31:770–790
    [Google Scholar]
  9. Van Heijenoort J., Parquet C., Flouret B., Van Heijenoort Y. 1975; Envelope-bound N-acetyl-muramyl-l-alanine amidase of Escherichia coli K-12. European Journal of Biochemistry 58:611–619
    [Google Scholar]
  10. Ingram L. O. 1981; Mechanism of lysis of Escherichia coli by ethanol and other chaotropic agents. Journal of Bacteriology 146:331–336
    [Google Scholar]
  11. Ishiguro E. E., Ramey W. D. 1976; Stringent control of peptidoglycan biosynthesis in Escherichia coli K-12. Journal of Bacteriology 127:1119–1126
    [Google Scholar]
  12. Kitano K., Tomasz A. 1979a; Escherichia coli mutants tolerant to beta lactam antibiotics. Journal of Bacteriology 140:955–963
    [Google Scholar]
  13. Kitano K., Tomasz A. 1979b; Triggering of autolytic cell wall degradation in Escherichia coli by beta-lactam antibiotics. Antimicrobial Agents and Chemotherapy 16:838–848
    [Google Scholar]
  14. Kitano K., Williamson R., Tomasz A. 1980; Murein hydrolase defect in beta lactam tolerant mutants of Escherichia coli. FEMS Microbiology Letters 1:133–136
    [Google Scholar]
  15. Markwell M. A. K, Haas S. M., Bieber L. L., Tolbert N. E. 1978; A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Analytical Biochemistry 87:206–210
    [Google Scholar]
  16. Miller J. H. 1972 Experimental Molecular Genetics. New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
  17. Mirelman D. 1979; Biosynthesis and assembly of cell wall peptidoglycan. In Bacterial Outer Membranes. Biogenesis and Functions pp. 115–166 Inouye M. Edited by New York: John Wiley & Sons;
    [Google Scholar]
  18. Noguchi H., Matsuhashi M., Mitsuhashi S. 1979; Comparative studies of penicillin-binding proteins in Pseudomonas aeruginosa and Escherichia coli. European Journal of Biochemistry 100:41–49
    [Google Scholar]
  19. Primosigh J., Pelzer H., Maas D. 1961; Chemical characterization of mucopeptides released from the E. coli B cell wall by enzymic action. Biochimica et biophysica acta 46:68–80
    [Google Scholar]
  20. Tomasz A. 1979; The mechanism of the irreversible antimicrobial effects of penicillins: how the beta- lactam antibiotics kill and lyse bacteria. Annual Review of Microbiology 33:113–137
    [Google Scholar]
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