Characterization of Elongation Factor Tu from Bacillus Subtilis Modified by Affinity Labelling

  • Jiří Jonák
  • Karel Karas
  • Ivan Rychlík


The ability of aminoacyl-tRNA to complex with elongation factor Tu is essential since the ternary complex EF-Tu.GTP.aminoacyl-tRNA is the way aminoacyl-tRNA is carried to the A site of mRNA-programmed ribosomes. During the reaction, GTP in the complex is hydrolysed to GDP, and a stable form of EF-Tu.GDP, which has a low affinity for aminoacyl-tRNA, is released from the ribosome (Kaziro, 1978). The role of GTP might be described as that of an effector which controls the function of the protein binding site for aminoacyl-tRNA.


Amino Acid Composition Elongation Factor Protein Binding Site Relative Molecular Mass Cysteic Acid 
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  1. Duffy, L. K., Gerber, L., Johnson, A. E., and Miller, D. L., 1981, Biochemistry, 20:4663.PubMedCrossRefGoogle Scholar
  2. Jonák, J., Smrt, J. A., Holý, A., and Rychlík, I., 1980, Eur. J. Biochem., 105:315.PubMedCrossRefGoogle Scholar
  3. Jonák, J., Petersen, T. E., Clark, B. F. C., and Rychlík, I., 1982, FEBS Lett., 150:485.PubMedCrossRefGoogle Scholar
  4. Jonák, J., Petersen, T. E., Meloun, B., and Rychlík, I., 1984, Eur. J. Biochem., 144:295.PubMedCrossRefGoogle Scholar
  5. Jonák, J., Pokorna, K., Meloun, B., and Karas, K., 1986, Eur. J. Biochem., 154:355.PubMedCrossRefGoogle Scholar
  6. Jones, M. D., Petersen, T. E., Nielsen, K. M., Magnusson, S., Sottrup-Jensen, L., Gausing, K., Clark, B. F. C., 1980, Eur. J. Biochem., 108:507.PubMedCrossRefGoogle Scholar
  7. Jurnak, F., 1985, Science, 230:32.PubMedCrossRefGoogle Scholar
  8. Kaziro, Y., 1978, Biochim. Biophys. Acta, 505:95.Google Scholar
  9. Knowlton, R. G., and Yarus, M., 1980, J. Mol. Biol., 139:721.Google Scholar
  10. La Cour, T. F. M., Nyborg, J., Thirup, S., and Clark, B. F. C., 1985, EMBO J., 4:2385.PubMedGoogle Scholar
  11. Miller, D. L., Hachmann, J., and Weissbach, H., 1971, Arch. Biochem. Biophys., 144:115.PubMedCrossRefGoogle Scholar
  12. Pingoud, A., and Urbanke, C., 1980, Biochemistry, 19:2108.PubMedCrossRefGoogle Scholar
  13. Richman, N., and Bodley, J. W., 1973, J. Biol. Chem., 248:381.PubMedGoogle Scholar
  14. Sedláček, J., Jonák, J., and Rychlík, I., 1971, Biochim. Biophys. Acta, 254:478.PubMedCrossRefGoogle Scholar
  15. Sedlíček, J., Rychlík, I., and Jonák, J., 1974, Biochim. Biophys. Acta, 349:78.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Jiří Jonák
    • 1
  • Karel Karas
    • 1
  • Ivan Rychlík
    • 1
  1. 1.Institute of Molecular GeneticsCzechoslovak Acad. Sci.Prague 6Czechoslovakia

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