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. 1964 Aug;88(2):297–308. doi: 10.1128/jb.88.2.297-308.1964

METABOLIC CONTROL OF PENICILLINASE BIOSYNTHESIS IN BACILLUS CEREUS1

Lily C Yip a, Ramesh Shah a, Richard A Day a
PMCID: PMC277299  PMID: 14203344

Abstract

Yip, Lily C. (University of Cincinnati, Cincinnati, Ohio), Ramesh Shah, and Richard A. Day. Metabolic control of penicillinase biosynthesis in Bacillus cereus. J. Bacteriol. 88:297–308. 1964.—Penicillinase production in strains 5 and 5/B of Bacillus cereus in response to treatment by 6-aminopenicillanic acid (APA), penicillin G, (6-N-α-(p-benzyloxyphenoxy)-propionylamino-penicillanic acid, and cephalosporin C (CC) was found to be analogous to that seen in constitutive strains. Strain 5 did not release penicillinase into the medium to any great extent. Penicillinase production and the effect of the above penicillins on it were found to decline with increasing density of the culture. The penicillins were shown to accelerate or retard the production of penicillinase activity in strain 5 cells during pretreatment at 0 C and during incubation at 37 C. Strains 5 and 5/B gave qualitatively similar responses to penicillin treatment. At 0 C, the specific activity of penicillinase in strain 5 passes through a period of rapid increase at 0 hr and a period of little change at approximately 1 hr, followed by an increased rate of change towards 2 hr. The effect of APA or CC on specific activity of strain 5 cells during treatment at 0 C could not be reversed by one another, but Hg could reverse the increase caused by CC to some extent and the repression caused by APA. The production of penicillinase in the microconstitutive strain 5 of Bacillus cereus in response to treatment with CC was influenced by various inhibitors. 8-Azaguanine inhibited the production of the enzyme both during a pretreatment of the cells with CC at 0 C and during the subsequent incubation at 37 C. Actinomycin D, 6-azauracil, 6-thioguanine, and 2-thiocytosine inhibit the increase in penicillinase arising after the pretreatment at 0 C. 6-Azathymine has very little effect on the change of penicillinase activity. The CC-induced change occurring during the 0 C period was postulated to be a process at the level of protein biosynthesis itself; change at 37 C, constituting a delayed response, was considered a process at the level of messenger ribonucleic acid synthesis.

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Selected References

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

  1. AMOS H., VOLLMAYER E., KORN M. Thiouridylic acid formation and bacterial growth. Arch Biochem Biophys. 1958 Sep;77(1):236–238. doi: 10.1016/0003-9861(58)90062-6. [DOI] [PubMed] [Google Scholar]
  2. CHANTRENNE H., LECLERCQ-CALINGAERT M. Secondary effect of 8-azaguanine on the induced or constitutive synthesis of penicillinase in Bacillus cereus. Biochim Biophys Acta. 1963 May 28;72:87–91. [PubMed] [Google Scholar]
  3. COOPER P. D. Site of action of radiopenicillin. Bacteriol Rev. 1956 Mar;20(1):28–48. doi: 10.1128/br.20.1.28-48.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DAY R. A., SHAH R. Penicillinase production in some bacilli. Science. 1962 Dec 7;138(3545):1108–1109. doi: 10.1126/science.138.3545.1108. [DOI] [PubMed] [Google Scholar]
  5. GARBER N., CITRI N. The interaction of penicillinase with penicillins. I. Effect of substrates and of a competitive inhibitor on native and urea-treated enzyme. Biochim Biophys Acta. 1962 Aug 13;62:385–396. doi: 10.1016/0006-3002(62)90268-8. [DOI] [PubMed] [Google Scholar]
  6. GORINI L., GUNDERSEN W. Induction by arginine of enzymes of arginine biosynthesis in Escherichia coli B. Proc Natl Acad Sci U S A. 1961 Jul 15;47:961–971. doi: 10.1073/pnas.47.7.961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. GORINI L. Symposium on multiple forms of enzymes and control mechanisms. III. Control by repression of a biochemical pathway. Bacteriol Rev. 1963 Jun;27:182–190. doi: 10.1128/br.27.2.182-190.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HAMERS R. Incorporation of 35S thiouracil in Bacillus megaterium. Biochim Biophys Acta. 1956 Jul;21(1):170–171. doi: 10.1016/0006-3002(56)90109-3. [DOI] [PubMed] [Google Scholar]
  9. HAUGE J. G., MACQUILLAN A. M., CLINE A. L., HALVORSON H. O. The effect of glucose repression on the level of ribosomalbound beta-glucosidase. Biochem Biophys Res Commun. 1961 Jul 26;5:267–269. doi: 10.1016/0006-291x(61)90160-7. [DOI] [PubMed] [Google Scholar]
  10. Hayashi M., Spiegelman S., Franklin N. C., Luria S. E. SEPARATION OF THE RNA MESSAGE TRANSCRIBED IN RESPONSE TO A SPECIFIC INDUCER. Proc Natl Acad Sci U S A. 1963 May;49(5):729–736. doi: 10.1073/pnas.49.5.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MACQUILLAN A. M., HALVORSON H. O. Metabolic control of beta-glucosidase synthesis in yeast. J Bacteriol. 1962 Jul;84:23–30. doi: 10.1128/jb.84.1.23-30.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MATTHEWS R. E., SMITH J. D. Distribution of 8-azaguanine in the nucleic acids of Bacillus cereus. Nature. 1956 Feb 11;177(4502):271–272. doi: 10.1038/177271a0. [DOI] [PubMed] [Google Scholar]
  13. MCFALL E., MANDELSTAM J. SPECIFIC METABOLIC REPRESSION OF THREE INDUCED ENZYMES IN ESCHERICHIA COLI. Biochem J. 1963 Nov;89:391–398. doi: 10.1042/bj0890391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. OHTAKA Y., SPIEGELMAN S. TRANSLATIONAL CONTROL OF PROTEIN SYNTHESIS IN A CELL-FREE SYSTEM DIRECTED BY A POLYCISTRONIC VIRAL RNA. Science. 1963 Oct 25;142(3591):493–497. doi: 10.1126/science.142.3591.493. [DOI] [PubMed] [Google Scholar]
  15. PERRET C. J. Iodometric assay of penicillinase. Nature. 1954 Nov 27;174(4439):1012–1013. doi: 10.1038/1741012a0. [DOI] [PubMed] [Google Scholar]
  16. POLLOCK M. R. A simple method for the production of high titre penicillinase. J Pharm Pharmacol. 1957 Sep;9(9):609–611. doi: 10.1111/j.2042-7158.1957.tb12316.x. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. 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]
  19. POLLOCK M. R. THE DIFFERENTIAL EFFECT OF ACTINOMYCIN D ON THE BIOSYNTHESIS OF ENZYMES IN BACILLUS SUBTILIS AND BACILLUS CEREUS. Biochim Biophys Acta. 1963 Sep 17;76:80–93. [PubMed] [Google Scholar]
  20. POLLOCK M. R. The activity and specificity of inducers of penicillinase production in Bacillus cereus, strain NRRL 569. Biochem J. 1957 Jul;66(3):419–428. doi: 10.1042/bj0660419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. POLLOCK M. R. The cell-bound penicillinase of Bacillus cereus. J Gen Microbiol. 1956 Aug;15(1):154–169. doi: 10.1099/00221287-15-1-154. [DOI] [PubMed] [Google Scholar]
  22. SCHEPARTZ S. A., JOHNSON M. J. The nature of the binding of penicillin by bacterial cells. J Bacteriol. 1956 Jan;71(1):84–90. doi: 10.1002/path.1700710112. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. SKODA J., SORM F. Accumulation of nucleic acid metabolites in Escherichia coli exposed to the action of 6-azauracil. Biochim Biophys Acta. 1958 Jun;28(3):659–660. doi: 10.1016/0006-3002(58)90544-4. [DOI] [PubMed] [Google Scholar]
  24. SNEATH P. H. Proof of the spontaneity of a mutation to penicillinase production in Bacillus cereus. J Gen Microbiol. 1955 Dec;13(3):561–568. doi: 10.1099/00221287-13-3-561. [DOI] [PubMed] [Google Scholar]
  25. SPIEGELMAN S. Information transfer from the genome. Fed Proc. 1963 Jan-Feb;22:36–54. [PubMed] [Google Scholar]
  26. Szilard L. THE CONTROL OF THE FORMATION OF SPECIFIC PROTEINS IN BACTERIA AND IN ANIMAL CELLS. Proc Natl Acad Sci U S A. 1960 Mar;46(3):277–292. doi: 10.1073/pnas.46.3.277. [DOI] [PMC free article] [PubMed] [Google Scholar]

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