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. 1979 Nov;140(2):643–648. doi: 10.1128/jb.140.2.643-648.1979

Lysis of Escherichia coli mutants by lactose.

J K Alexander
PMCID: PMC216692  PMID: 40961

Abstract

Growth of Escherichia coli strain MM6-13 (ptsI suc lacI sup), which as a suppressor of the succinate-negative phenotype, was inhibited by lactose. Cells growing in yeast extract-tryptone-sodium chloride medium (LB broth) were lysed upon the addition of lactose. In Casamino Acids-salts medium, lactose inhibited growth, but due to the high K+ content no lysis occurred. Lysis required high levels of beta-galctosidase and lactose transport activity. MM6, the parental strain of MM6-13, has lower levels of both of these activities and was resistant to lysis under these conditions. When MM6 was grown in LB broth with exogenous cyclic adenosine monophosphate, however, beta-galactosidase and lactose transport activities were greatly increased, and lysis occurred upon the addition of lactose. Resting cells of both MM6 and MM6-13 were lysed by lactose in buffers containing suitable ions. In the presence of MG2+, lysis was enhanced by 5 mM KCl and 100 mM NaCl. Higher slat concentrations (50 mM KCl or 200 mM NaCl) provided partial protection from lysis. In the absence of Mg2+, lysis occurred without KCl. Lactose-dependent lysis occurred in buffers containing anions such as sulafte, chloride, phosphate, or citrate; however, thiocyanate or acetate protected the cells from lysis. These data indicate that both cations and anions, as well as the levels of lactose transport and beta-galactosidase activity, are important in lysis.

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Selected References

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

  1. Alexander J. K., Tyler B. Genetic analysis of succinate utilization in enzyme I mutants of the phosphoenolpyruvate: sugar phosphotransferase system in Escherichia coli. J Bacteriol. 1975 Oct;124(1):252–261. doi: 10.1128/jb.124.1.252-261.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Kennedy C. K. Induction of colicin production by high temperature or inhibition of protein synthesis. J Bacteriol. 1971 Oct;108(1):10–19. doi: 10.1128/jb.108.1.10-19.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Leive L. Studies on the permeability change produced in coliform bacteria by ethylenediaminetetraacetate. J Biol Chem. 1968 May 10;243(9):2373–2380. [PubMed] [Google Scholar]
  4. Lo T. C., Rayman M. K., Sanwal B. D. Transport of succinate in Escherichia coli. I. Biochemical and genetic studies of transport in whole cells. J Biol Chem. 1972 Oct 10;247(19):6323–6331. [PubMed] [Google Scholar]
  5. SOLS A., DE LA FUENTE G. Hexokinase and other enzymes of sugar metabolism in the intestine. Methods Med Res. 1961;9:302–309. [PubMed] [Google Scholar]
  6. Wang R. J., Morse H. G., Morse M. L. Carbohydrate Accumulation and Metabolism in Escherichia coli: Characteristics of the Reversions of ctr Mutations. J Bacteriol. 1970 Dec;104(3):1318–1324. doi: 10.1128/jb.104.3.1318-1324.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]

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