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. 1975 Jul;8(1):38–44. doi: 10.1128/aac.8.1.38

Accessibility of the [14C]Benzylpenicillin Binding Proteins in Membranes of Sporulating Bacilli

Thomas E Hamilton 1, Paul J Lawrence 1
PMCID: PMC429257  PMID: 809003

Abstract

Triton X-100 treatment or freeze-thawing damages the membranes of sporulating or vegetative cells as seen by protein leakage from cells. A 40% increase in the specific [14C]benzylpenicillin-binding capacity of detergent-treated or frozen sporulating cells was observed. Neither freezing nor Triton X-100 treatment of vegetative cells produced a detectable effect on their [14C]benzylpenicillin-binding capacity. These data indicate the presence of penicillin-binding sites in intact sporulating bacilli not accessible to penicillin in routine binding assays. The chemical specificity of [14C]benzylpenicillin binding to detergent-treated sporulating cells is similar to that observed with untreated vegetative or sporulating cells.

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Selected References

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

  1. Blumberg P. M., Strominger J. L. Five penicillin-binding components occur in Bacillus subtilis membranes. J Biol Chem. 1972 Dec 25;247(24):8107–8113. [PubMed] [Google Scholar]
  2. Chow C. T., Takahashi I. Acid-soluble nucleotides in an asporogenous mutant of Bacillus subtilis. J Bacteriol. 1972 Mar;109(3):1175–1180. doi: 10.1128/jb.109.3.1175-1180.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hitchins A. D., Slepecky R. A. Antibiotic inhibition of the septation stage in sporulation of Bacillus megaterium. J Bacteriol. 1969 Mar;97(3):1513–1515. doi: 10.1128/jb.97.3.1513-1515.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hitchins A. D., Slepecky R. A. Bacterial sporulation as a modified procaryotic cell division. Nature. 1969 Aug 23;223(5208):804–807. doi: 10.1038/223804a0. [DOI] [PubMed] [Google Scholar]
  5. Izaki K., Matsuhashi M., Strominger J. L. Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions. Proc Natl Acad Sci U S A. 1966 Mar;55(3):656–663. doi: 10.1073/pnas.55.3.656. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Johnson D. A., Mania D. Epi-6-aminopenicillanic acid and epipenicillin G. Tetrahedron Lett. 1969 Jan;(4):267–270. doi: 10.1016/s0040-4039(01)87526-2. [DOI] [PubMed] [Google Scholar]
  7. KOLODZIEJ B. J., SLEPECKY R. A. TRACE METAL REQUIREMENTS FOR SPORULATION OF BACILLUS MEGATERIUM. J Bacteriol. 1964 Oct;88:821–830. doi: 10.1128/jb.88.4.821-830.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Lawrence P. J. Penicillin: reversible inhibition of forespore septum development in Bacillus megaterium cells. Antimicrob Agents Chemother. 1974 Dec;6(6):815–820. doi: 10.1128/aac.6.6.815. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lawrence P. J., Rogolsky M., Hanh V. T. Binding of radioactive benzylpenicillin to sporulating Bacillus cultures: chemistry and fluctuations in specific binding capacity. J Bacteriol. 1971 Nov;108(2):662–667. doi: 10.1128/jb.108.2.662-667.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lawrence P. J., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. XV. The binding of radioactive penicillin to the particulate enzyme preparation of Bacillus subtilis and its reversal with hydroxylamine or thiols. J Biol Chem. 1970 Jul 25;245(14):3653–3659. [PubMed] [Google Scholar]
  12. Lawrence P. J., Strominger J. L. Biosynthesis of the peptidoglycan of bacterial cell walls. XVI. The reversible fixation of radioactive penicillin G to the D-alanine carboxypeptidase of Bacillus subtilis. J Biol Chem. 1970 Jul 25;245(14):3660–3666. [PubMed] [Google Scholar]
  13. PRUESS D. L., JOHNSON M. J. ENZYMATIC DEACYLATION OF S35-BENZYLPENICILLIN. J Bacteriol. 1965 Aug;90:380–383. doi: 10.1128/jb.90.2.380-383.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pearce S. M., Fitz-James P. C. Sporulation of a cortexless mutant of a variant of Bacillus cereus. J Bacteriol. 1971 Jan;105(1):339–348. doi: 10.1128/jb.105.1.339-348.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rogolsky M., Lawrence P. J., Hanh V. T. Binding of radioactive benzylpenicillin to asporogenous mutants of Bacillus subtilis during postexponential growth. J Bacteriol. 1973 Apr;114(1):220–227. doi: 10.1128/jb.114.1.220-227.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schmid R., Plapp R. Binding of 14 C-penicillin G to Proteus mirabilis. Arch Mikrobiol. 1972;83(3):246–260. doi: 10.1007/BF00645125. [DOI] [PubMed] [Google Scholar]
  17. Storm D. R., Blumberg P. M., Strominger J. L. Inhibition of the Bacillus subtilis membrane-bound D-alanine carboxypeptidase by 6-aminopenicillanic acid covalently coupled to sepharose. J Bacteriol. 1974 Feb;117(2):783–785. doi: 10.1128/jb.117.2.783-785.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Vinter V. Spores of microorganisms. XVII. The fate of preexisting diaminopimelic acid-containing structures during germination and postgerminative development of bacterial spores. Folia Microbiol (Praha) 1965 Sep;10(5):280–287. doi: 10.1007/BF02871027. [DOI] [PubMed] [Google Scholar]

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