1887

Abstract

Four penicillin-binding proteins (PBPs) were observed in the soluble fraction of CB13, and designated PBP S1 (mol. wt 60000), PBP S2 (55000), PBP S3 (45000) and PBP S4 (40000). CB15, an independent isolate, possessed similar soluble PBPs, but not PBP S2. These soluble PBPs could be observed even when a cell suspension was directly reacted with [C]penicillin G. Two of the soluble PBPs, S1 and S2, released half their bound [C]penicillin G during a 10 min incubation, indicating that these PBPs have penicillinase-like activity. PBP S2 was very thermolabile and lost its penicillin-binding activity after incubation at 40 °C for 10 min. Mecillinam did not show selective binding to any of the soluble PBPs or to PBPs in the cell envelope.

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/content/journal/micro/10.1099/00221287-128-5-1117
1982-05-01
2021-07-30
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References

  1. Bonner W. M., Laskey R. A. 1974; A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. European Journal of Biochemistry 46:83–88
    [Google Scholar]
  2. Chase H. A., Reynolds P. E., Ward J. B. 1978; Purification and characterization of the penicillinbinding protein that is the lethal target of penicillin in Bacillus megaterium and Bacillus licheniformis. Protein exchange and complex stability. European Journal of Biochemistry 88:275–285
    [Google Scholar]
  3. Coyette J., Ghuysen J.-M., Fontana R. 1980; The penicillin-binding proteins in Streptococcus faecalis ATCC 9790. European Journal of Biochemistry 110:445–456
    [Google Scholar]
  4. Curtis N. A. C., Orr D., Ross G. W., Boulton M. G. 1979; Competition of β-lactam antibiotics for the penicillin-binding proteins of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli: comparison with anti-bacterial activity and effects upon bacterial morphology. Antimicrobial Agents and Chemotherapy 16:325–328
    [Google Scholar]
  5. Iba H., Okada Y. 1980; Chromosome segregation in an asymmetrically dividing bacterium, Caulobacter crescentus . Journal of Molecular Biology 139:733–739
    [Google Scholar]
  6. Iwaya M., Goldman R., Tipper D. J., Feingold B., Strominger J. L. 1978; Morphology of an Escherichia coli mutant with a temperature-dependent round cell shape. Journal of Bacteriology 136:1143–1158
    [Google Scholar]
  7. Johnson R. C., Ely B. 1977; Isolation of spontaneously derived mutants of Caulobacter crescentus . Genetics 86:25–32
    [Google Scholar]
  8. Koyasu S., Fukuda A., Okada Y. 1980a; The penicillin-binding proteins of Caulobacter crescentus . Journal of Biochemistry 87:363–366
    [Google Scholar]
  9. Koyasu S., Fukuda A., Okada Y. 1980b; Penicillin-binding proteins in soluble fraction of Escherichia coli K-12. Proceedings of the Japan Academy(Series B) 56:420–424
    [Google Scholar]
  10. Koyasu S., Fukuda A., Okada Y. 1981; Properties of the penicillin-binding proteins of Caulobacter . Journal of General Microbiology 126:111–121
    [Google Scholar]
  11. Laskey R. A., Mills A. D. 1975; Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. European Journal of Biochemistry 56:335–341
    [Google Scholar]
  12. Leyh-Bouille M., Dusart J., Nguyen-Distèche M., Ghuysen J.-M., Reynolds P. E., Perkins H. R. 1977; The peptidoglycan crosslinking enzyme system in Streptomyces strains R61, K15 and rimosus. Exocellular, lysozyme-releasable and membrane-bound enzymes. European Journal of Biochemistry 81:19–28
    [Google Scholar]
  13. Nakagawa J., Matsuzawa H., Matsuhashi M. 1979; Behavior of penicillin-binding proteins in Escherichia coli upon heat and detergent treatments and partial purification of penicillin-binding proteins 1A and IB. Journal of Bacteriology 138:1029–1032
    [Google Scholar]
  14. 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]
  15. Ogawara H., Horikawa S. 1980; Penicillinbinding proteins of Streptomyces cacaoi, Streptomyces olivaceus, and Streptomyces clavuligerus . Antimicrobial Agents and Chemotherapy 17:1–7
    [Google Scholar]
  16. Ohya S., Yamazaki M., Sugawara S., Matsuhashi M. 1979; Penicillin-binding proteins in Proteus species. Journal of Bacteriology 137:474–479
    [Google Scholar]
  17. Poindexter J. S. 1964; Biological properties and classification of the Caulobacter group. Bacteriological Reviews 28:231–295
    [Google Scholar]
  18. Poindexter J. S. 1981; The caulobacters: ubiquitous unusual bacteria. Microbiological Reviews 45:123–179
    [Google Scholar]
  19. Shapiro L. 1976; Differentiation in the Caulobacter cell cycle. Annual Review of Microbiology 30:377–407
    [Google Scholar]
  20. Shepherd S. T., Chase H. A., Reynolds P. E. 1977; The separation and properties of two penicillin-binding proteins from Salmonella typhi-murium . European Journal of Biochemistry 78:521–532
    [Google Scholar]
  21. Spratt B. G. 1975; Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proceedings of the National Academy of Sciences of the United States of America 72:2999–3003
    [Google Scholar]
  22. Spratt B. G. 1977a; Properties of the penicillinbinding proteins of Escherichia coli K12. European Journal of Biochemistry 72:341–352
    [Google Scholar]
  23. Spratt B. G. 1977b; Temperature-sensitive cell division mutants of Escherichia coli with thermolabile penicillin-binding proteins. Journal of Bacteriology 131:293–305
    [Google Scholar]
  24. Spratt B. G., Pardee A. B. 1975; Penicillinbinding proteins and cell shape in E. coli . Nature; London: 254516–517
    [Google Scholar]
  25. Suzuki H., Nishimura Y., Hirota Y. 1978; On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillinbinding proteins. Proceedings of the National Academy of Sciences of the United States of America 75:654–668
    [Google Scholar]
  26. Tamaki S., Nakajima S., Matsuhashi M. 1977; Thermosensitive mutation in Escherichia coli simul-taneously causing defects in penicillin-binding protein-IBs and in enzyme activity for peptidoglycan synthesis in vitro . Proceedings of the National Academy of Sciences of the United States of America 74:5472–5476
    [Google Scholar]
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