Molecular Biology Reports

, Volume 3, Issue 2, pp 105–111 | Cite as

Further evidence for the participation of proteins S 3, S 14 and S 19 in tRNA binding to E. coli 30 S subunits

  • Marilyn Shimizu
  • Gary R. Craven


Previous studies have shown that iodination of 30 S subunits causes inactivation for both enzymatic fMet-tRNA and non-enzymatic phe-tRNA binding activities. This inactivation was shown to be due to the modification of three to five ribosomal proteins [1]. In this report the role of these proteins in tRNA binding activity has been further studied. Purified ribosomal proteins, isolated from modified subunits, are re-assembled into otherwise unmodified 30 S ribosomes and assayed for tRNA binding capacity. The presence of modified S 3, S 14 and S 19 (S 15) in the reconstituted particle results in substantial reduction of both fMet-tRNA and phe-tRNA binding activities. This reduction in tRNA binding activity does not appear to be due to an assembly defect.


Ribosomal Protein Binding Activity Binding Capacity Substantial Reduction Assembly Defect 
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. 1.
    Shimizu, M. and Craven, G. R., Eur. J. Biochem. 61, 307 (1975).Google Scholar
  2. 2.
    Held, W. A., Mizushima, S., and Nomura, M., J. Biol. Chem. 218, 5720 (1973).Google Scholar
  3. 3.
    Thomas, G., Sweeney, R., Chang, C., and Noller, H. F., J. Mol. Biol. 95, 91 (1975).Google Scholar
  4. 4.
    Kahan, L., Held, W.A., and Nomura, M., J. Mol. Biol. 88, 797 (1974).Google Scholar
  5. 5.
    Dubnoff, J. S. and Maitra, U., in K. Moldave and L. Grossman (eds.), Methods in Enzymology XX, Part C, Academic Press, Inc., New York, 1971, pp. 248–261.Google Scholar
  6. 6.
    Hochkeppel, H. K., Spicer, E., and Craven, G. R., J. Mol. Biol. 101, 155 (1976).Google Scholar
  7. 7.
    Hardy, S. J. S., Kurland, C. G., Voynow, P., and Mora, G., Biochemistry 8, 2897 (1969).Google Scholar
  8. 8.
    Smolarsky, M. and Tal, M., Biochim. Biophys. Acta 199, 447 (1970).Google Scholar
  9. 9.
    Last, J. A., in J. A. Last and A. I. Laskin (eds.), Protein Biosynthesis in Bacterial Systems, Marcel Dekker, Inc., New York, 1971, pp. 151–176.Google Scholar
  10. 10.
    Voynow, P. and Kurland, C. G., Biochemistry, 10, 517 (1970).Google Scholar
  11. 11.
    Wittman, H. G., Stöffler, G., Hindennach, I., Kurland, C. G., Randall-Hazelbauer, L., Birge, E. A., Nomura, M., Kaltschmidt, E., Mizushima, S., Traut, R. R., and Bickle, T. A., Mol. Gen. Genet. 111, 327 (1971).Google Scholar

Copyright information

© D. Reidel Publishing Company 1976

Authors and Affiliations

  • Marilyn Shimizu
    • 1
    • 2
  • Gary R. Craven
    • 1
    • 2
  1. 1.The Laboratory of Molecular BiologyThe University of WisconsinMadisonUSA
  2. 2.the Department of GeneticsThe University of WisconsinMadisonUSA

Personalised recommendations