1887

Abstract

Summary: The distributions of penicillinase in populations of uninduced, induced and constitutive cultures of strains 749 and 749/c each showed a large positive skew. Analysis of the enzyme distribution in the uninduced population as a Poisson distribution showed that penicillinase molecules were produced not as independent random events, but in clusters containing 1100 molecules. There were 0.4 (average 0.85) clusters/organism. The fundamental random event resulting in the formation of a cluster of penicillinase molecules may be the formation of one enzyme-forming site capable of producing 1100 such molecules. Analysis of the enzyme distribution in the constitutive population showed that in this case penicillinase was produced in groups of 55,000 molecules, or fifty of the clusters of penicillinase found in the organisms of the uninduced population. This may be the number of enzyme-forming sites made by a constitutive penicillinase gene during the period between its formation and replication. Analysis of the enzyme distribution in the induced population showed that the organisms did not respond equally after induction, but all organisms probably increased their rates of penicillinase synthesis. Enzyme partition can be highly asymmetric when an organism divides; the enzyme molecules do not appear to be able to diffuse freely within the cell cytoplasm, but may be associated with some structurally rigid material in the organisms.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-34-3-363
1964-03-01
2024-04-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/34/3/mic-34-3-363.html?itemId=/content/journal/micro/10.1099/00221287-34-3-363&mimeType=html&fmt=ahah

References

  1. Benzer S. 1953; Induced synthesis of enzymes in bacteria analyzed at the cellular level. Biochim. biophys. Acta 11:383
    [Google Scholar]
  2. Cohn M., Horibata K. 1959a; Inhibition by glucose of the induced synthesis of the β-galactoside-enzyme system of Escherichia coli. Analysis of maintenance. J. Bact 78:601
    [Google Scholar]
  3. Cohn M., Horibata K. 1959b; Analysis of the differentiation and of the heterogeneity within a population of Escherichia coli undergoing induced β-galactosidase synthesis. J. Bact 78:613
    [Google Scholar]
  4. Collins J. F. 1962; Estimation of penicillinase in single bacterial cells. Biochem. J 82:28 p
    [Google Scholar]
  5. Collins J. F., Kornberg H. L. 1960; The metabolism of C2 compounds in microorganisms. Biochem. J 77:430
    [Google Scholar]
  6. Collins J. F., Mason D. B., Perkins W. J. 1964; A microphotometric method for the estimation of penicillinase in single bacterial cells. J. gen. Microbiol 34:353
    [Google Scholar]
  7. Collins J. F., Richmond M. H. 1962; Rate of growth of Bacillus cereus between divisions. J. gen. Microbiol 28:15
    [Google Scholar]
  8. Kogut M., Pollock M. R., Tridgell E. J. 1956; Purification of penicillin-induced penicillinase of Bacillus cereus nrrl569; a comparison of its properties with those of a similarly purified penicillinase produced spontaneously by a constitutive mutant. Biochem. J 62:391
    [Google Scholar]
  9. Kushner D. J. 1960; An immunological study of Bacillus subtilis penicillinases. J. gen. Microbiol 23:381
    [Google Scholar]
  10. Kushner D. J., Pollock M. R. 1961; The location of cell-bound penicillinase in Bacillus subtilis . J. gen. Microbiol 26:255
    [Google Scholar]
  11. Jacob F., Monod J. 1961; Genetic regulatory mechanisms in the synthesis of proteins. J. molec. Biol 3:318
    [Google Scholar]
  12. Manson E. E., Pollock M. R., Tridgell E. J. 1954; A comparison of the properties of penicillinase produced by Bacillus subtilis and Bacillus cereus with and without addition of penicillin. J. gen. Microbiol 11:493
    [Google Scholar]
  13. Novick A., Weiner M. 1957; Enzyme induction as an all-or-none phenomenon. Proc. not. Acad. Sci., Wash 43:553
    [Google Scholar]
  14. Novick R. P. 1962; Micro-iodometric assay for penicillinase. Biochem. J 83:236
    [Google Scholar]
  15. Novick R. P. 1963; Analysis by transduction of mutations affecting penicillinase formation in Staphylococcus aureus . J. gen. Microbiol 33:121
    [Google Scholar]
  16. Perret C. J. 1954; Iodometric assay of penicillinase. Nature, Lond 174:1012
    [Google Scholar]
  17. Pollock M. R., Perret C. J. 1951; The relation between the fixation of penicillin- sulphur and pencillinase adaptation in B. cereus . Brit. J. exp. Path 32:387
    [Google Scholar]
  18. Wright H. D. 1933; The importance of adequate reduction of peptone in the preparation of media for the Pneumococcus and other organisms. J. Path. Bact 37:257
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-34-3-363
Loading
/content/journal/micro/10.1099/00221287-34-3-363
Loading

Data & Media loading...

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