Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1994 Mar;60(3):785–791. doi: 10.1128/aem.60.3.785-791.1994

Production of Bacteriolytic Enzymes by Streptomyces globisporus Regulated by Exogenous Bacterial Cell Walls

Volker Brönneke 1, Franz Fiedler 1,*
PMCID: PMC201393  PMID: 16349213

Abstract

Mutanolysin biosynthesis and pigment production in Streptomyces globisporus ATCC 21553 were stimulated by adding bacterial cell walls to the medium. The increased bacteriolytic activity in the supernatant correlated with an increased de novo synthesis of mutanolysin and was between 4- and 20-fold higher than in cultures grown without bacterial cell walls. The increase in mutanolysin synthesis was brought about by enhanced transcription of the mutanolysin gene. The stimulation was only observed in medium which contained dextrin or starch as the carbon source. Glucose abolished the stimulation and also inhibited the low constitutive synthesis of mutanolysin. The induction of lytic activity was observed to require minimally 0.4 mg of bacterial cell walls per ml, whereas 0.6 mg of bacterial cell walls per ml yielded maximal lytic activity. Further supplements of bacterial cell walls did not result in enhanced lytic activity. The stimulation could be achieved independently of the phase of growth of the Streptomyces strain. Cultures grown in the presence of bacterial cell walls exhibited a higher growth yield. However, the accelerated growth was not the reason for the increased amount of mutanolysin produced. The growth of cultures with peptidoglycan monomers added to the medium instead of cell walls was similarly increased, but an effect on the biosynthesis of mutanolysin was not observed. All bacterial cell walls tested were capable of eliciting the stimulation of lytic activity, including cell walls of archaea, which contained pseudomurein.

Full text

PDF
785

Images in this article

787Image
on p.787
789Image
on p.789

Selected References

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

  1. 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]
  2. Bräu B., Hilgenfeld R., Schlingmann M., Marquardt R., Birr E., Wohlleben W., Aufderheide K., Pühler A. Increased yield of a lysozyme after self-cloning of the gene in Streptomyces coelicolor "Müller". Appl Microbiol Biotechnol. 1991 Jan;34(4):481–487. doi: 10.1007/BF00180575. [DOI] [PubMed] [Google Scholar]
  3. Chater K. F. Genetic regulation of secondary metabolic pathways in Streptomyces. Ciba Found Symp. 1992;171:144–162. doi: 10.1002/9780470514344.ch9. [DOI] [PubMed] [Google Scholar]
  4. Cheong J. J., Hahn M. G. A specific, high-affinity binding site for the hepta-beta-glucoside elicitor exists in soybean membranes. Plant Cell. 1991 Feb;3(2):137–147. doi: 10.1105/tpc.3.2.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cosio E. G., Pöpperl H., Schmidt W. E., Ebel J. High-affinity binding of fungal beta-glucan fragments to soybean (Glycine max L.) microsomal fractions and protoplasts. Eur J Biochem. 1988 Aug 1;175(2):309–315. doi: 10.1111/j.1432-1033.1988.tb14198.x. [DOI] [PubMed] [Google Scholar]
  6. Demain A. L. Microbial secondary metabolism: a new theoretical frontier for academia, a new opportunity for industry. Ciba Found Symp. 1992;171:3–23. doi: 10.1002/9780470514344.ch2. [DOI] [PubMed] [Google Scholar]
  7. Eckerskorn C., Mewes W., Goretzki H., Lottspeich F. A new siliconized-glass fiber as support for protein-chemical analysis of electroblotted proteins. Eur J Biochem. 1988 Oct 1;176(3):509–519. doi: 10.1111/j.1432-1033.1988.tb14308.x. [DOI] [PubMed] [Google Scholar]
  8. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
  9. Fiedler F., Kandler O. Die Aminosäuresequenz von 2,4-diaminobuttersäure enthaltenden Mureinen bei verschiedenen coryneformen Bakterien und Agromyces ramosus. Arch Mikrobiol. 1973;89(1):51–66. [PubMed] [Google Scholar]
  10. Fiedler F., Schleifer K., Kandler O. Amino acid sequence of the threonine-containing mureins of coryneform bacteria. J Bacteriol. 1973 Jan;113(1):8–17. doi: 10.1128/jb.113.1.8-17.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fujii T., Miyashita K. Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans. J Gen Microbiol. 1993 Apr;139(4):677–686. doi: 10.1099/00221287-139-4-677. [DOI] [PubMed] [Google Scholar]
  12. Glauner B., Höltje J. V., Schwarz U. The composition of the murein of Escherichia coli. J Biol Chem. 1988 Jul 25;263(21):10088–10095. [PubMed] [Google Scholar]
  13. Harada S., Kitadokoro K., Fujii T., Kai Y., Kasai N. Preliminary X-ray crystallographic study of lysozyme produced by Streptomyces globisporus. J Mol Biol. 1989 Jun 20;207(4):851–852. doi: 10.1016/0022-2836(89)90254-4. [DOI] [PubMed] [Google Scholar]
  14. Kandler O., König H. Chemical composition of the peptidoglycan-free cell walls of methanogenic bacteria. Arch Microbiol. 1978 Aug 1;118(2):141–152. doi: 10.1007/BF00415722. [DOI] [PubMed] [Google Scholar]
  15. Kuhn M., Goebel W. Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells. Infect Immun. 1989 Jan;57(1):55–61. doi: 10.1128/iai.57.1.55-61.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Lichenstein H. S., Hastings A. E., Langley K. E., Mendiaz E. A., Rohde M. F., Elmore R., Zukowski M. M. Cloning and nucleotide sequence of the N-acetylmuramidase M1-encoding gene from Streptomyces globisporus. Gene. 1990 Mar 30;88(1):81–86. doi: 10.1016/0378-1119(90)90062-v. [DOI] [PubMed] [Google Scholar]
  18. Schleifer K. H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev. 1972 Dec;36(4):407–477. doi: 10.1128/br.36.4.407-477.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Schleifer K. H., Kandler O. Zur chemischen Zusammensetzung der Zellwand der Streptokokken. I. Die Aminosäuresequenz des Mureins von Str. thermophilus und Str. faecalis. Arch Mikrobiol. 1967 Jul 6;57(4):335–364. [PubMed] [Google Scholar]
  20. Schleifer K. H., Kocur M. Classification of staphylococci based on chemical and biochemical properties. Arch Mikrobiol. 1973 Oct 4;93(1):65–85. doi: 10.1007/BF00666081. [DOI] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES