Skip to main content
PMC home page
Antimicrobial Agents and Chemotherapy logoLink to Antimicrobial Agents and Chemotherapy
. 1974 Dec;6(6):734–740. doi: 10.1128/aac.6.6.734

Induction Kinetics of β-Lactamase Biosynthesis in Pseudomonas aeruginosa

Kurt Nordström 1,2, Richard B Sykes 1,2,1
PMCID: PMC444728  PMID: 4217583

Abstract

The induction of β-lactamase in Pseudomonas aeruginosa 1822s was studied using benzylpenicillin as inducer. The specific rate of β-lactamase formation was constant throughout an induction experiment. Above a threshold (20 μg/ml), the specific activity increased linearly with the concentration of the inducer. Removal of the inducer resulted in a rapid cessation of β-lactamase biosynthesis. Inhibition of protein synthesis by starvation for a required amino acid or by the addition of chloramphenicol also led to an instantaneous arrest in enzyme formation. In the absence of inducer, a basal β-lactamase activity was formed. The basal and the induced enzymes seem to be identical since they had the same substrate profile, electrophoretic mobility, and molecular weight. In all these respects, induction of β-lactamase in Pseudomonas aeruginosa is analogous to induction of the lac operon in Escherichia coli. However, there was a long, concentration-dependent lag before β-lactamase was induced. This can be explained by the outer penetration barrier decreasing the rate of inducer uptake. The lag was significantly shorter for lysozyme-ethylenediaminetetraacetic acid-produced spheroplasts than for intact cells. Induction was obtained with all β-lactam antibiotics tested, but not with other agents affecting the cell envelope.

Full text

PDF
734

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BENZER S. Induced synthesis of enzymes in bacteria analyzed at the cellular level. Biochim Biophys Acta. 1953 Jul;11(3):383–395. doi: 10.1016/0006-3002(53)90057-2. [DOI] [PubMed] [Google Scholar]
  2. BERTANI G. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol. 1951 Sep;62(3):293–300. doi: 10.1128/jb.62.3.293-300.1951. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bryan L. E., Van Den Elzen H. M., Tseng J. T. Transferable drug resistance in Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1972 Jan;1(1):22–29. doi: 10.1128/aac.1.1.22. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burman L. G., Nordström K., Bloom G. D. Murein and the outer penetration barrier of Escherichia coli K-12, Proteus mirabilis, and Pseudomonas aeruginosa. J Bacteriol. 1972 Dec;112(3):1364–1374. doi: 10.1128/jb.112.3.1364-1374.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. COLLINS J. F. THE DISTRIBUTION AND FORMATION OF PENICILLINASE IN A BACTERIAL POPULATION OF BACILLUS LICHENIFORMIS. J Gen Microbiol. 1964 Mar;34:363–377. doi: 10.1099/00221287-34-3-363. [DOI] [PubMed] [Google Scholar]
  6. Csányi V., Jacobi G., Straub B. F. The regulation of penicillinase synthesis. Biochim Biophys Acta. 1967 Sep 26;145(2):470–484. doi: 10.1016/0005-2787(67)90065-2. [DOI] [PubMed] [Google Scholar]
  7. Datta N., Richmond M. H. The purification and properties of a penicillinase whose synthesis is mediated by an R-factor in Escherichia coli. Biochem J. 1966 Jan;98(1):204–209. doi: 10.1042/bj0980204. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Garber N., Friedman J. Beta-lactamase and the resistance of Pseudomonas aeruginosa to various penicillins and cephalosporins. J Gen Microbiol. 1970 Dec;64(3):343–352. doi: 10.1099/00221287-64-3-343. [DOI] [PubMed] [Google Scholar]
  9. HERZENBERG L. A. Studies on the induction of beta-galactosidase in a cryptic strain of Escherichia coli. Biochim Biophys Acta. 1959 Feb;31(2):525–538. doi: 10.1016/0006-3002(59)90029-0. [DOI] [PubMed] [Google Scholar]
  10. Hamilton-Miller J. M. Damaging effects of ethylenediaminetetra-acetate and penicillins on permeability barriers in Gram-negative bacteria. Biochem J. 1966 Sep;100(3):675–682. doi: 10.1042/bj1000675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hochstadt Ozer J., Lowery D. L., Saz A. K. Derepression of beta-lactamase (penicillinase in Bacillus cereus by peptidoglycans. J Bacteriol. 1970 Apr;102(1):52–63. doi: 10.1128/jb.102.1.52-63.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Imsande J., Zyskind J. W., Mile I. Regulation of staphylococcal penicillinase synthesis. J Bacteriol. 1972 Jan;109(1):122–133. doi: 10.1128/jb.109.1.122-133.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. JACOB F., MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318–356. doi: 10.1016/s0022-2836(61)80072-7. [DOI] [PubMed] [Google Scholar]
  14. JAGO M., MIGLIACCI A., ABRAHAM E. P. PRODUCTION OF A CEPHALOSPORINASE BY PSEUDOMONAS PYOCYANEA. Nature. 1963 Jul 27;199:375–375. doi: 10.1038/199375a0. [DOI] [PubMed] [Google Scholar]
  15. Jack G. W., Richmond M. H. A comparative study of eight distinct beta-lactamases synthesized by gram-negative bacteria. J Gen Microbiol. 1970 Apr;61(1):43–61. doi: 10.1099/00221287-61-1-43. [DOI] [PubMed] [Google Scholar]
  16. Koch A. L., Deppe C. S. In vivo assay of protein synthesizing capacity of Escherichia coli from slowly growing chemostat cultures. J Mol Biol. 1971 Feb 14;55(3):549–562. doi: 10.1016/0022-2836(71)90336-6. [DOI] [PubMed] [Google Scholar]
  17. Koch A. L. The adaptive responses of Escherichia coli to a feast and famine existence. Adv Microb Physiol. 1971;6:147–217. doi: 10.1016/s0065-2911(08)60069-7. [DOI] [PubMed] [Google Scholar]
  18. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  19. Lindqvist R. C., Nordström K. Resistance of Escherichia coli to penicillins. VII. Purification and characterization of a penicillinase mediated by the R factor R1. J Bacteriol. 1970 Jan;101(1):232–239. doi: 10.1128/jb.101.1.232-239.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Lindström E. B., Nordström K. Automated method for determination of penicillins, cephalosporins, and penicillinases. Antimicrob Agents Chemother. 1972 Feb;1(2):100–106. doi: 10.1128/aac.1.2.100. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Linström E. B., Boman H. G., Steele B. B. Resistance of Escherichia coli to penicillins. VI. Purification and characterization of the chromosomally mediated penicillinase present in ampA-containing strains. J Bacteriol. 1970 Jan;101(1):218–231. doi: 10.1128/jb.101.1.218-231.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. MONOD J., PAPPENHEIMER A. M., Jr, COHEN-BAZIRE G. La cinétique de la biosynthèse de la beta-galactosidase chez E. coli considérée comme fonction de la croissance. Biochim Biophys Acta. 1952 Dec;9(6):648–660. doi: 10.1016/0006-3002(52)90227-8. [DOI] [PubMed] [Google Scholar]
  23. Neu H. C. The surface localization of penicillinases in Escherichia coli and Salmonella typhimurium. Biochem Biophys Res Commun. 1968 Jul 26;32(2):258–263. doi: 10.1016/0006-291x(68)90378-1. [DOI] [PubMed] [Google Scholar]
  24. Nordström K., Eriksson-Grennberg K. G., Boman H. G. Resistance of Escherichia coli to penicillins. 3. AmpB, a locus affecting episomally and chromosomally mediated resistance to ampicillin and chlorampheincol. Genet Res. 1968 Oct;12(2):157–168. doi: 10.1017/s0016672300011770. [DOI] [PubMed] [Google Scholar]
  25. PARDEE A. B., PRESTIDGE L. S. The initial kinetics of enzyme induction. Biochim Biophys Acta. 1961 Apr 29;49:77–88. doi: 10.1016/0006-3002(61)90871-x. [DOI] [PubMed] [Google Scholar]
  26. POLLOCK M. R., PERRET C. J. The relation between fixation of penicillin sulphur and penicillinase adaptation in B cereus. Br J Exp Pathol. 1951 Oct;32(5):387–396. [PMC free article] [PubMed] [Google Scholar]
  27. POLLOCK M. R. Penicillinase adaptation in B. cereus; adaptive enzyme formation in the absence of free substrate. Br J Exp Pathol. 1950 Dec;31(6):739–753. [PMC free article] [PubMed] [Google Scholar]
  28. Richmond M. H. Enzymic adaptation in bacteria: its biochemical and genetic basis. Essays Biochem. 1968;4:105–154. [PubMed] [Google Scholar]
  29. Richmond M. H., Sykes R. B. The beta-lactamases of gram-negative bacteria and their possible physiological role. Adv Microb Physiol. 1973;9:31–88. doi: 10.1016/s0065-2911(08)60376-8. [DOI] [PubMed] [Google Scholar]
  30. Rosselet A., Zimmermann W. Mutants of Pseudomonas aeruginosa with impaired -lactamase inducibility and increased sensitivity to -lactam antibiotics. J Gen Microbiol. 1973 Jun;76(2):455–457. doi: 10.1099/00221287-76-2-455. [DOI] [PubMed] [Google Scholar]
  31. SMITH J. T. Penicillinase and ampicillin resistance in a strain of Escherichia coli. J Gen Microbiol. 1963 Feb;30:299–306. doi: 10.1099/00221287-30-2-299. [DOI] [PubMed] [Google Scholar]
  32. Sabath L. D., Finland M. Resistance of penicillins and cephalosporins to beta-lactamases from Gram-negative bacilli: some correlations with antibacterial activity. Ann N Y Acad Sci. 1967 Sep 27;145(2):237–247. doi: 10.1111/j.1749-6632.1967.tb50222.x. [DOI] [PubMed] [Google Scholar]
  33. Sabath L. D., Jago M., Abraham E. P. Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea. Biochem J. 1965 Sep;96(3):739–752. doi: 10.1042/bj0960739. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Sykes R. B., Richmond M. H. Intergeneric transfer of a beta-lactamase gene between Ps. aeruginosa and E. coli. Nature. 1970 Jun 6;226(5249):952–954. doi: 10.1038/226952a0. [DOI] [PubMed] [Google Scholar]
  35. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  36. von Meyenburg Kaspar Transport-limited growth rates in a mutant of Escherichia coli. J Bacteriol. 1971 Sep;107(3):878–888. doi: 10.1128/jb.107.3.878-888.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Antimicrobial Agents and Chemotherapy are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES