Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1964 Dec;88(6):1567–1572. doi: 10.1128/jb.88.6.1567-1572.1964

MECHANISM OF RESISTANCE TO ACTINOMYCIN IN BACILLUS SUBTILIS

M Polsinelli 1, O Ciferri 1, G Cassani 1, A Albertini 1
PMCID: PMC277453  PMID: 14240938

Abstract

Polsinelli, M. (University of Pavia, Pavia, Italy), O. Ciferri, G. Cassani, and A. Albertini. Mechanism of resistance to actinomycin in Bacillus subtilis. J. Bacteriol. 88:1567–1572. 1964.—Strains of Bacillus subtilis were rendered resistant to actinomycin D by serial transfer in increasing concentrations of the drug. Resistance to the antibiotic appeared to be due to an altered cell-wall permeability, because the resistant strains did not take up actinomycin. No evidence was found for the presence of an enzyme(s) degrading actinomycin. Deoxyribonucleic acid (DNA) extracted from the actinomycin-resistant strains was found to bind actinomycin to the same extent as the DNA extracted from susceptible strains. The genetic nature of the resistance to actinomycin was demonstrated by means of transformation. Resistant strains appeared to have almost completely lost their transformability, as well as the tendency to autolyze.

Full text

PDF
1567

Selected References

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

  1. Bondi A., Dietz C. C. The Susceptibility of Penicillinase-producing Bacteria to Penicillin: I. Factors Influencing Susceptibility. J Bacteriol. 1948 Jun;55(6):843–847. [PMC free article] [PubMed] [Google Scholar]
  2. DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. EPHRATI-ELIZUR E., SRINIVASAN P. R., ZAMENHOF S. Genetic analysis, by means of transformation, of histidine linkage groups in Bacillus subtilis. Proc Natl Acad Sci U S A. 1961 Jan 15;47:56–63. doi: 10.1073/pnas.47.1.56. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. HANCOCK R. Uptake of 14C-streptomycin by some microorganisms and its relation to their streptomycin sensitivity. J Gen Microbiol. 1962 Jul;28:493–501. doi: 10.1099/00221287-28-3-493. [DOI] [PubMed] [Google Scholar]
  5. HAYWOOD A. M., SINSHEIMER R. L. Inhibition of protein synthesis in E. coli protoplasts by actinomycin-D. J Mol Biol. 1963 Mar;6:247–249. doi: 10.1016/s0022-2836(63)80074-1. [DOI] [PubMed] [Google Scholar]
  6. HURWITZ J., FURTH J. J., MALAMY M., ALEXANDER M. The role of deoxyribonucleic acid in ribonucleic acid synthesis. III. The inhibition of the enzymatic synthesis of ribonucleic acid and deoxyribonucleic acid by actinomycin D and proflavin. Proc Natl Acad Sci U S A. 1962 Jul 15;48:1222–1230. doi: 10.1073/pnas.48.7.1222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KIRK J. M. The mode of action of actinomycin D. Biochim Biophys Acta. 1960 Jul 29;42:167–169. doi: 10.1016/0006-3002(60)90769-1. [DOI] [PubMed] [Google Scholar]
  8. KUSHNER D. J. The basis of chloramphenicol resistance in Pseudomonas fluorescens. Arch Biochem Biophys. 1955 Oct;58(2):347–355. doi: 10.1016/0003-9861(55)90134-x. [DOI] [PubMed] [Google Scholar]
  9. LEVINTHAL C., KEYNAN A., HIGA A. Messenger RNA turnover and protein synthesis in B. subtilis inhibited by actinomycin D. Proc Natl Acad Sci U S A. 1962 Sep 15;48:1631–1638. doi: 10.1073/pnas.48.9.1631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. MARTINEZ L. M., SAZ A. K. Enzymatic basis of resistance to aureomycin. I. Differences between flavoprotein nitro reductases of sensitive and resistant Escherichia coli. J Biol Chem. 1956 Nov;223(1):285–292. [PubMed] [Google Scholar]
  11. NESTER E. W., LEDERBERG J. Linkage of genetic units of Bacillus subtilis in DNA transformation. Proc Natl Acad Sci U S A. 1961 Jan 15;47:52–55. doi: 10.1073/pnas.47.1.52. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. RAUEN H. M., KERSTEN H., KERSTEN W. [On the mode of action of actinomycins]. Hoppe Seylers Z Physiol Chem. 1960 Dec 2;321:139–147. doi: 10.1515/bchm2.1960.321.1.139. [DOI] [PubMed] [Google Scholar]
  13. REICH E., FRANKLIN R. M., SHATKIN A. J., TATUMEL Action of actinomycin D on animal cells and viruses. Proc Natl Acad Sci U S A. 1962 Jul 15;48:1238–1245. doi: 10.1073/pnas.48.7.1238. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. SIROTNAK F. M., LUNT R. B., HUTCHISON D. J. ALTERATION IN TRANSFORMABILITY OF DIPLOCOCCUS PNEUMONIAE AFTER THE ACQUISITION OF GENETIC DETERMINANTS INDUCING RESISTANCE TO ERYTHROMYCIN. J Bacteriol. 1963 Oct;86:735–739. doi: 10.1128/jb.86.4.735-739.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Spizizen J. TRANSFORMATION OF BIOCHEMICALLY DEFICIENT STRAINS OF BACILLUS SUBTILIS BY DEOXYRIBONUCLEATE. Proc Natl Acad Sci U S A. 1958 Oct 15;44(10):1072–1078. doi: 10.1073/pnas.44.10.1072. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. YOUNG F. E., SPIZIZEN J. BIOCHEMICAL ASPECTS OF COMPETENCE IN THE BACILLUS SUBTILIS TRANSFORMATION SYSTEM. II. AUTOLYTIC ENZYME ACTIVITY OF CELL WALLS. J Biol Chem. 1963 Sep;238:3126–3130. [PubMed] [Google Scholar]
  17. YOUNG F. E., SPIZIZEN J. Physiological and genetic factors affecting transformation of Bacillus subtilis. J Bacteriol. 1961 May;81:823–829. doi: 10.1128/jb.81.5.823-829.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES