Archiv für Mikrobiologie

, Volume 57, Issue 4, pp 382–387 | Cite as

Effect of antibiotics on ribosomal RNA and proteins from Streptococcus pyogenes

  • Bohdan Bubela
  • George F. Scrimshaw
  • David F. Oberhauser


Cells of Streptococcus pyogenes were prepared under rigid conditions. The microorganisms were then incubated for 3 hours in the presence or absence of chloramphenicol, actinomycin or puromycin. RNA, ribosomal fraction and ribosomal proteins were isolated from the cells. The materials were invesigated with the help of infra red spectroscopy using the potassium bromide pellet method. Quantitative differences in the 1750–1500 cm-1 region were observed with materials treated with the antibiotics. Synthetic mixtures of ribosomal RNA with progressively larger amounts of ribosomal proteins show analogous changes, namely a progressive increase in the strength of the 1650 cm-1 band relative to the 1685 cm-1 band, and an increase in the 1535 cm-1 band. The analytical results obtained with the ribosomal RNA isolated from S. pyogenes treated with antibiotics indicated increased amounts of proteins which could not be removed by the applied extraction method. The evidence presented suggests a change in the binding between ribosomal RNA and ribosomal proteins in the material isolated from the antibiotic treated microorganisms. The I. R. spectroscopy seems to be an useful tool in the investigation of some aspects of biological materials.


Chloramphenicol Ribosomal Protein Quantitative Difference Actinomycin Puromycin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Acs, G., E. Reich, and S. Valanju: RNA metabolism in B. subtilis: Effect of actinomycin. Biochim. biophys. Acta (Amst.) 76, 68 (1963).Google Scholar
  2. Allen, D. W., and P. C. Zamecnik: The effect of puromycin on rabbit reticulocytes ribosomes. Biochim. biophys. Acta (Amst.) 55, 865 (1962).Google Scholar
  3. Bubela, B., and D. F. Oberhauser: An automatic apparatus for inoculating, growing and harvesting of microorganisms. Biotechnol. Bioeng. 8, 453 (1966).Google Scholar
  4. Burton, D., and G. B. Petersen: The frequences of certain sequences of nucleotides in deoxyribonucleic acid. Biochem. J. 75, 17 (1960).Google Scholar
  5. Caspi, E., and G. F. Scrimshaw: In: Qualitative and quantitative analysis of steroid hormones, H. Carstensen, ed., New York: M. Dekker Inc. 1967.Google Scholar
  6. Cook, E. S., C. W. Kreke, E. B. Barnes, and W. Motzel: Infra red and ultra violet absorption spectra of proteins in the solid state. Nature (Lond.) 174, 1144 (1954).Google Scholar
  7. Creaser, E. H.: The induced (adaptive) biosynthesis of β-galactosidase in S. aureus. J. gen. Microbiol. 12, 288 (1955).Google Scholar
  8. Crestfield, A. M., K. C. Smith, and F. W. Allen: The preparation and characterisation of ribonucleic acids from yeast. J. biol. Chem. 216, 185 (1955).Google Scholar
  9. Hosokawa, K., and M. Nomura: Biosynthesis of ribosomes: Fate of chloramphenicol particles and pulse labeled RNA in Escherichia coli. J. molec. Biol. 12, 242 (1965).Google Scholar
  10. Lowry, O. N.: Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265 (1951).Google Scholar
  11. McNiven, N. L.: In: Laboratory methods in infrared spectroscopy, R. G. J. Miller ed., p. 91. Spectrum House, London: Heyden Press 1965.Google Scholar
  12. Rao, C. N. R.: In: Chemical applications of infrared spectroscopy. New York: Academic Press 1963.Google Scholar
  13. Revel, M., H. H. Hiat, and J. Revel: Actinomycin D: An effect on liver homogenates uncorelated to its action of RNA syntheses. Science 146, 1311 (1964).Google Scholar
  14. Scrimshaw, G. F., B. Bubela, and D. F. Oberhauser: Effect of puromycin on ribosomal particles from S. pyogenes. Life Sci. 5, 1743 (1966).Google Scholar
  15. Shimanouchi, T., M. Tsuboi, and Y. Kyogoku: Infra red spectra of nucleic acids and related compounds, p. 435. In: Advances in Chemical Physics, Vol. VII. The structure and properties of biomolecules and biological systems, J. Duchesne, ed. New York: Interscience Publ. 1964.Google Scholar
  16. Waller, J. P., and J. T. Karris: Studies on the composition of the protein from E. coli ribosomes. Proc. nat. Acad. Sci. (Wash.). 47, 18 (1961).Google Scholar
  17. Wolfe, A. D., and F. E. Hahn: Mode of action of chloramphenicol. IX. Effects of chloramphenicol upon ribosomes and its binding to bacterial ribosomes. Biochim. biophys. Acta (Amst.) 95, 146 (1965).Google Scholar
  18. Yarmolinsky, M. B., and G. L. de la Haba: Inhibition by puromycin of amino acids incorporation into proteins. Proc. nat. Acad. Sci. (Wash.). 45, 1721 (1959).Google Scholar

Copyright information

© Springer-Verlag 1967

Authors and Affiliations

  • Bohdan Bubela
    • 1
    • 2
  • George F. Scrimshaw
    • 1
  • David F. Oberhauser
    • 1
  1. 1.Worcester Foundation for Experimental BiologyShrewsburyMassachusettsUSA
  2. 2.Baas-Becking Geobiological Research LaboratoriesC.S.I.R.O.CanberraAustralia

Personalised recommendations