Molecular and General Genetics MGG

, Volume 152, Issue 3, pp 239–243 | Cite as

Further temperature-sensitive mutants ofEscherichia coli with altered ribosomal proteins

  • Katsumi Isono
  • A. Garth Cumberlidge
  • Setsuko Isono
  • Yukinori Hirota


Various alterations in ribosomal proteins were detected in forty-one mutants ofE. coli isolated as temperature-sensitive mutants. Out of these, six are new classes of mutants harboring mutations in proteins S3, L5, L7 (L12), L29, L30 and L33. One of them apparently lacks protein L7 of the large subunit. These mutants together with those reported previously (Isono et al., 1976) total one hundred and one ribosomal mutants in thirty different proteins.


Ribosomal Protein Large Subunit ofEscherichia Coli Ribosomal Mutant 
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  1. Apirion, D., Schlessinger, D., Phillips, S., Sypherd, P.:Escherichia coli: Reversion from streptomycin dependence, a mutation in a specific 30S ribosomal protein. J. molec. Biol.43, 327–329 (1969)Google Scholar
  2. Dabbs, E. R., Wittmann, H. G.: A strain ofE. coli which gives rise to mutants in a large number of ribosomal proteins. Molec. gen. Genet.149, 303–309 (1976)Google Scholar
  3. Funatsu, G., Puls, W., Schiltz, E., Reinbolt, J., Wittmann, H. G.: Ribosomal proteins. XXXI. Comparative studies on altered proteins S4 of sixEscherichia coli revertants from streptomycin dependence. Molec. gen. Genet.115, 131–139 (1972)Google Scholar
  4. Garvin, R. T., Rosset, R., Gorini, L.: Ribosomal assembly influenced by growth in the presence of streptomycin. Proc. nat. Acad. Sci. (Wash.)70, 2762–2766 (1973)Google Scholar
  5. Hamel, E., Koka, M., Nakamoto, T.: Requirement of anEscherichia coli 50S ribosomal protein component for effective interaction of the ribosome with T and G factor and with guanosine triphosphate. J. biol. Chem.247, 805–814 (1972)Google Scholar
  6. Hasenbank, R., Guthrie, C., Stöffler, G., Wittmann, H. G., Rosen, L., Apirion, D.: Electrophoretic and immunological studies on ribosomal proteins of 100Escherichia coli revertants from streptomycin dependence. Molec. gen. Genet.127, 1–18 (1973)Google Scholar
  7. Isono, K., Krauss, J., Hirota, Y.: Isolation and characterization of temperature-sensitive mutants ofEscherichia coli with altered ribosomal proteins. Molec. gen. Genet.149, 297–302 (1976)Google Scholar
  8. Kaltschmidt, E., Wittmann, H.G.: Ribosomal proteins. VII. Twodimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins. Analyt. Biochem.36, 401–412 (1970)Google Scholar
  9. Olsson, M., Isaksson, L., Kurland, C.G.: Pleiotropic effects of ribosomal proteins S4 studied inEscherichia coli mutants. Molec. gen. Genet.135, 191–202 (1974)Google Scholar
  10. Ramagopal, S., Subramanian, A. R.: Growth-dependent regulation in production and utilization of acetylated ribosomal protein L7. J. molec. Biol.94, 633–641 (1975)Google Scholar
  11. Reimbolt, J., Schiltz, E.: The primary structure of ribosomal protein S4 fromEscherichia coli. FEBS Letters36, 250–252 (1973)Google Scholar
  12. Rosset, R., Vola, C., Feunteun, J., Monier, R.: A thermosensitive mutant defective in ribosomal 30S subunit assembly. FEBS Letters18, 127–129 (1971)Google Scholar

Copyright information

© Springer-Verlag 1977

Authors and Affiliations

  • Katsumi Isono
    • 1
  • A. Garth Cumberlidge
    • 1
  • Setsuko Isono
    • 1
  • Yukinori Hirota
    • 2
  1. 1.Abt. WittmannMax-Planck-Institut für Molekulare GenetikBerlin 33
  2. 2.National Institute of GeneticsMishimaJapan

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