Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1973 Oct;116(1):123–130. doi: 10.1128/jb.116.1.123-130.1973

Resistance of Escherichia coli to Penicillins: Identification of the Structural Gene for the Chromosomal Penicillinase

Lars G Burman a,1, James T Park a,2, E Börje Lindström a, Hans G Boman a
PMCID: PMC246399  PMID: 4200837

Abstract

A screening procedure was used to isolate a number of mutants of Escherichia coli K-12 with low penicillinase activity. By co-transduction with purA, three of the mutants were found to map near 82 min. Penicillinase was purified from one mutant and from a transductant with a temperature-sensitive enzyme. Comparison with wild-type penicillinase revealed similarities in the Ouchterlony immunodiffusion test but differences in the catalytic properties. It is concluded that the mutations have occurred in the structural gene of the chromosomal penicillinase (designated ampC). Purified enzyme and a temperature-sensitive mutant were used to investigate whether the penicillinase has a physiological function related to biosynthesis or breakdown of murein. No positive evidence for any such function was obtained.

Full text

PDF
123

Images in this article

127Image
on p.127
128Image
on p.128

Selected References

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

  1. 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]
  2. Braun V., Rehn K. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur J Biochem. 1969 Oct;10(3):426–438. doi: 10.1111/j.1432-1033.1969.tb00707.x. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Burman L. G., Nordström K., Boman H. G. Resistance of Escherichia coli to penicillins. V. Physiological comparison of two isogenic strains, one with chromosomally and one with episomally mediated ampicillin resistance. J Bacteriol. 1968 Aug;96(2):438–446. doi: 10.1128/jb.96.2.438-446.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dubnau D. A., Pollock M. R. The genetics of Bacillus licheniformis penicillinase: a preliminary analysis from studies on mutation and inter-strain and intra-strain transformations. J Gen Microbiol. 1965 Oct;41(1):7–21. doi: 10.1099/00221287-41-1-7. [DOI] [PubMed] [Google Scholar]
  6. Eriksson-Grennberg K. G., Boman H. G., Jansson J. A., Thorén S. Resistance of Escherichia coli to Penicillins I. Genetic Study of Some Ampicillin-Resistant Mutants. J Bacteriol. 1965 Jul;90(1):54–62. doi: 10.1128/jb.90.1.54-62.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eriksson-Grennberg K. G. Resistance of Escherichia coli to penicillins. II. An improved mapping of the ampA gene. Genet Res. 1968 Oct;12(2):147–156. doi: 10.1017/s0016672300011769. [DOI] [PubMed] [Google Scholar]
  8. Hartmann R., Höltje J. V., Schwarz U. Targets of penicillin action in Escherichia coli. Nature. 1972 Feb 25;235(5339):426–429. doi: 10.1038/235426a0. [DOI] [PubMed] [Google Scholar]
  9. Hata T., Omura S., Iwai Y., Ono H., Takeshima H. Studies on penicillinase inhibitors produced by microorganisms. J Antibiot (Tokyo) 1972 Aug;25(8):473–474. doi: 10.7164/antibiotics.25.473. [DOI] [PubMed] [Google Scholar]
  10. INGRAM V. M. Gene mutations in human haemoglobin: the chemical difference between normal and sickle cell haemoglobin. Nature. 1957 Aug 17;180(4581):326–328. doi: 10.1038/180326a0. [DOI] [PubMed] [Google Scholar]
  11. Izaki K., Matsuhashi M., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. 8. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of Escherichia coli. J Biol Chem. 1968 Jun 10;243(11):3180–3192. [PubMed] [Google Scholar]
  12. 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]
  13. 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]
  14. NOVICK R. P. ANALYSIS BY TRANSDUCTION OF MUTATIONS AFFECTING PENICILLINASE FORMATION IN STAPHYLOCOCCUS AUREUS. J Gen Microbiol. 1963 Oct;33:121–136. doi: 10.1099/00221287-33-1-121. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. POLLOCK M. R. An immunological study of the constitutive and the penicillin-induced penicillinases of Bacillus cereus, based on specific enzyme neutralization by antibody. J Gen Microbiol. 1956 Feb;14(1):90–108. doi: 10.1099/00221287-14-1-90. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Smith D. H., Davis B. D. Mode of action of novobiocin in Escherichia coli. J Bacteriol. 1967 Jan;93(1):71–79. doi: 10.1128/jb.93.1.71-79.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Taylor A. L. Current linkage map of Escherichia coli. Bacteriol Rev. 1970 Jun;34(2):155–175. doi: 10.1128/br.34.2.155-175.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]
  21. WEIDEL W., PELZER H. BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS. Adv Enzymol Relat Areas Mol Biol. 1964;26:193–232. doi: 10.1002/9780470122716.ch5. [DOI] [PubMed] [Google Scholar]
  22. Wise E. M., Jr, Park J. T. Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis. Proc Natl Acad Sci U S A. 1965 Jul;54(1):75–81. doi: 10.1073/pnas.54.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES