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Mutant E. coli Strain with Temperature Sensitive Peptidyltransfer RNA Hydrolase

Nature New Biology volume 240, pages 245–246 (1972)Cite this article

Abstract

WE have isolated a strain of Escherichia coli K-12 bacteria that we believe to be conditionally defective in peptidyl-tRNA hydrolase. This enzyme (which we shall refer to as hydrolase) catalyses the hydrolysis of peptidyl-tRNA (or N-acyl-amino-acyl-tRNA) yielding free peptide (or N-acyl-amino-acid) and a tRNA capable of accepting its conjugate amino-acid1,2. In the current model of protein biosynthesis3 peptidyl-tRNA is the form in which the growing protein is bound to the ribosome. Ribosome-bound peptidyl-tRNA, however, is a poor substrate for the hydrolase2,4, implying that the normal substrate is free. N-acyl-aminoacyl-tRNAs occur in cells5–7 but the only species the function of which is known3,8, N-formyl-methionyl-tRNAf, is a poor substrate for bacterial peptidyl-tRNA hydrolase1,9,10.

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References

  1. Lapidot, Y., and de Groot, N., in Progress in Nucleic Acid Research, 12, 189 (Academic Press, New York, 1972).

    Google Scholar 

  2. Menninger, J. R., Mulholland, M. C., and Stirewalt, W. S., Biochim. Biophys. Acta, 217, 496 (1970).

    Article  CAS  PubMed  Google Scholar 

  3. Lucas-Lenard, J., and Lipmann, F., Ann. Rev. Biochem., 40, 409 (1971).

    Article  CAS  PubMed  Google Scholar 

  4. de Groot, N., Panet, A., and Lapidot, Y., Biochem. Biophys. Res. Commun., 31, 37 (1968).

    Article  CAS  PubMed  Google Scholar 

  5. Marcker, K., and Sanger, F., J. Mol. Biol., 8, 835 (1964).

    Article  CAS  PubMed  Google Scholar 

  6. Kim, W. S., Science, 163, 947 (1969).

    Article  CAS  PubMed  Google Scholar 

  7. Liew, C. C., Haslett, G. W., and Allfrey, V. G., Nature, 226, 414 (1970).

    Article  CAS  PubMed  Google Scholar 

  8. Clark, B. F. C., and Marcker, K. A., Nature, 207, 1038 (1965).

    Article  CAS  PubMed  Google Scholar 

  9. Lapidot, Y., Inbar, D., de Groot, N., and Kössel, H., FEBS Lett., 3, 253 (1969).

    Article  CAS  PubMed  Google Scholar 

  10. Kössel, H., Biochim. Biophys. Acta, 204, 191 (1970).

    Article  PubMed  Google Scholar 

  11. Cuzin, F., Kretchmer, N., Greenberg, R. E., Hurwitz, R., ahd Chapeville, F., Proc. US Nat. Acad. Sci., 58, 2079 (1967).

    Article  CAS  Google Scholar 

  12. Kössel, H., and Raj Bhandary, U. L., J. Mol. Biol., 35, 539 (1968).

    Article  PubMed  Google Scholar 

  13. Raacke, I. D., Robins, H. I., Binder, K. S., and Jordan, R. E., Fed. Proc., 30, 1209 (1971).

    Google Scholar 

  14. Raacke, I. D., Proc. US Nat. Acad. Sci., 68, 2357 (1971).

    Article  CAS  Google Scholar 

  15. Atherly, A. G., and Suchanek, M. C., J. Bact., 108, 627 (1971).

    CAS  PubMed  PubMed Central  Google Scholar 

  16. Phillips, S. L., Schlessinger, D., and Apirion, D., Proc. US Nat. Acad. Sci., 62, 772 (1969).

    Article  CAS  Google Scholar 

  17. Matthai, J. H., and Nirenberg, M. W., Proc. US Nat. Acad. Sci., 47, 1580 (1961).

    Article  Google Scholar 

  18. Bretscher, M. S., Goodman, H. M., Menninger, J. R., and Smith, J. D., J. Mol. Biol., 14, 634 (1965).

    Article  CAS  PubMed  Google Scholar 

  19. Menninger, J. R., Biochim. Biophys. Acta, 240, 237 (1971).

    Article  CAS  PubMed  Google Scholar 

  20. Siegelman, F., and Apirion, D., J. Bact., 105, 902 (1971).

    CAS  PubMed  PubMed Central  Google Scholar 

  21. Taylor, A. L., Bact. Rev., 34, 155 (1970).

    CAS  PubMed  PubMed Central  Google Scholar 

  22. Taylor, A. L., and Trotter, C. D., Bact. Rev., 31, 332 (1967).

    CAS  PubMed  PubMed Central  Google Scholar 

  23. Guerola, N., Ingraham, J. L., and Cerdá-Olmedo, E., Nature New Biology, 230, 122 (1971).

    Article  CAS  PubMed  Google Scholar 

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Author notes

  1. JOHN R. MENNINGER

    Present address: Department of Zoology, University of Iowa, Iowa City, Iowa, 52240

Authors and Affiliations

  1. Department of Genetics, Iowa State University, Ames, Iowa, 50010

    ALAN G. ATHERLY

  2. Institute of Molecular Biology and Department of Biology, University of Oregon, Eugene, Oregon, 97403

    JOHN R. MENNINGER

Authors
  1. ALAN G. ATHERLY
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  2. JOHN R. MENNINGER
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ATHERLY, A., MENNINGER, J. Mutant E. coli Strain with Temperature Sensitive Peptidyltransfer RNA Hydrolase. Nature New Biology 240, 245–246 (1972). https://doi.org/10.1038/newbio240245a0

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  • DOI: https://doi.org/10.1038/newbio240245a0

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