1887

Abstract

ETH 22794 produced a variety of antibiotic substances. Besides low molecular weight antibiotics like hydroxystreptomycin and the tetracenomycins, this strain excreted glaucescin, a high molecular weight product with bacteriocin-like properties. In plate tests the antagonism of glaucescin against was masked by the large inhibition zone caused by the tetracenomycins. Glaucescin activity was revealed when a tetracenomycin-resistant mutant of NRRL 3155 was used as an indicator. Glaucescin was produced on complex and minimal solid and liquid media. It was not inducible by mitomycin C. The killing activity of glaucescin was thermolabile and resistant to DNAase, RNAase, various proteinases, and lipase. Its apparent molecular weight was estimated as 196000 by gel filtration and glycerol gradient centrifugation. Glaucescin preferentially killed outgrowing spores of Resting spores and mycelium were considerably less sensitive to the inhibitor, and adsorption of glaucescin by paralleled sensitivity. The activity spectrum of the bacteriocin was restricted to spore-forming Actinomycetales. Non spore-forming nocardiae and a variety of Gram-positive and Gram-negative bacteria were resistant to glaucescin.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-113-2-243
1979-08-01
2024-04-24
Loading full text...

Full text loading...

/deliver/fulltext/micro/113/2/mic-113-2-243.html?itemId=/content/journal/micro/10.1099/00221287-113-2-243&mimeType=html&fmt=ahah

References

  1. Andrews P. 1965; The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochemical Journal 96:595–606
    [Google Scholar]
  2. Baumann R., Kocher H.P. 1976; Genetics of Streptomyces glaucescens and regulation of melanin production. In 2nd International Symposium on the Genetics of Industrial Microorganisms pp. 535–551 Macdonald K.D. Edited by London: Academic Press.;
    [Google Scholar]
  3. Baumann R., Hütter R., Hopwood D.A. 1974; Genetic analysis in a melanin-producing streptomycete, Streptomyces glaucescens.. Journal of General Microbiology 81:463–474
    [Google Scholar]
  4. Bergmeyer H.U. 1974 Methoden der Enzymatischen Analyse, 3rd edn.. Weinheim: Verlag Chemie.;
    [Google Scholar]
  5. Bowman C.M., Sidikaro J., Nomura M. 1971; Specific inactivation of ribosomes by colicin E3 in vitro and mechanism of immunity in colicino-genic cell. Nature New Biology 234:133–137
    [Google Scholar]
  6. Bradley D.E. 1967; Ultrastructure of bacteriophages and bacteriocins. Bacteriological Reviews 31:230–314
    [Google Scholar]
  7. Eichenlaub R., Winkler U. 1974; Purification and mode of action of two bacteriocins produced by Serratia marcescens HY. Journal of General Microbiology 83:83–94
    [Google Scholar]
  8. Franker C.K., Herbert C.A., Ueda S. 1977; Bacteriocin from Actinomyces odontolyticus with temperature-dependent killing properties. Antimicrobial Agents and Chemotherapy 12:410–417
    [Google Scholar]
  9. Ganguly P., Das Gupta N.N., Chatterjea J.B. 1963; Sedimentation characteristics of the human haemoglobin A, F and E. Nature; London: 199919–920
    [Google Scholar]
  10. Goldin B.R., Frieden C. 1971; l-Glutamate dehydrogenases. Current Topics in Cellular Regulation 4:77–117
    [Google Scholar]
  11. Herbert D., Phipps P.J., Strange R.E. 1971; Chemical analysis of microbial cells. Methods in Microbiology 5B:209–344
    [Google Scholar]
  12. Hopwood D.A., Chater K.F., Dowding J.E., Vivian A. 1973; Advances in Streptomyces coelicolor genetics. Bacteriological Reviews 37:371–405
    [Google Scholar]
  13. Hunt D.E., Sandham H.J. 1969; Improved agar gradient plate technique. Applied Microbiology 17:329–330
    [Google Scholar]
  14. Hütter R. 1967 Systematik der Streptomyceten Basel: Karger.;
    [Google Scholar]
  15. Jaenicke R., Knof S. 1968; Molecular weight and quaternary structure of lactic dehydrogenase. European Journal of Biochemistry 4:157–163
    [Google Scholar]
  16. Kanarek L., Marler E., Bradshaw R.A., Fellows R.E., Hill R.L. 1964; The subunits of fumarase. Journal of Biological Chemistry 239:4207–4211
    [Google Scholar]
  17. Mahony D.E. 1977; Induction of bacteriocins from Clostridium perfringens by treatment with mitomycin C. Antimicrobial Agents and Chemotherapy 11:1067–1068
    [Google Scholar]
  18. Martin R.G., Ames B.N. 1961; A method for determining the sedimentation behaviour of enzymes: application to protein mixtures. Journal of Biological Chemistry 236:1372–1379
    [Google Scholar]
  19. Mayr-Harting A., Hedges A.J., Berkeley R.C.W. 1972; Methods for studying bacteriocins. Methods in Microbiology 7A:316–422
    [Google Scholar]
  20. Ouchi K., Kawase N., Nakano S., Akiyama H. 1978; Stabilization of yeast killer factor by glycerol. Agricultural and Biological Chemistry 42:1–5
    [Google Scholar]
  21. Pridham T.G., Lyons A.J. 1961; Streptomyces albus (Rossi Doria) Waksman et Henrici: taxonomic study of strains labelled Streptomyces albus.. Journal of Bacteriology 81:431–441
    [Google Scholar]
  22. Pridham T.G., Anderson P., Foley C., Linden-Felser L.A., Hesseltine C.W., Benedict R.G. 1957; A selection of media for maintenance and taxonomic studies of streptomycetes. Antibiotics Annual 1956/57:947–953
    [Google Scholar]
  23. Roelants P., Naudts F. 1964; Properties of a bacteriocin-like substance produced by Streptomyces virginiae.. Antonie van Leeuwenhoek 30:45–53
    [Google Scholar]
  24. Sober H.A. 1970 Handbook of Biochemistry. Selected Data for Molecular Biology, 2nd edn. pp. C3–C35 Cleveland: The Chemical Rubber Company.;
    [Google Scholar]
  25. Szybalsky W. 1952; Gradient plate technique for study of bacterial resistance. Science 116:46–47
    [Google Scholar]
  26. Tagg J.R., Dajani A.S., Wannamaker L.W. 1976; Bacteriocins of gram-positive bacteria. Bacteriological Reviews 40:722–756
    [Google Scholar]
  27. Weber W., Zaehner H., Siebers J., Schroeder K., Zeeck A. 1979; Stoffwechselprodukte von Mikroorganismen, 175. Mitteilung. Tetracenomycin C. Archives of Microbiology 121:111–116
    [Google Scholar]
  28. Wu J., Yang J.T. 1970; Physicochemical characterization of citrate synthase and its subunits. Journal of Biological Chemistry 245:212–218
    [Google Scholar]
  29. Yousten A.A., Rogoff M.H. 1969; Metabolism of Bacillus thuringiensis in relation to spore and crystal formation. Journal of Bacteriology 100:1229–1236
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-113-2-243
Loading
/content/journal/micro/10.1099/00221287-113-2-243
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error