Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Untersuchungen über Phagenlysozym

IV. Die molekulare Ursache des kälteempfindlichen Phänotyps der Mutante cseBU56 des Phagen T4D: Der Aminosäureaustausch Tyrosin 88 → Histidin

Studies on phage lysozyme

IV. The molecular cause of the cold-sensitive phenotype of the phage T4D mutant cseBU56: the amino acid substitution tyrosine 88 → histidine

  • 27 Accesses

  • 6 Citations

Summary

The structural basis of the cold-sensitive phenotype of the mutant cseBU56 is the amino acid substitution tyrosine 88 → histidine, resulting from a point mutation in the lysozyme gene of phage T4D. This was demonstrated by peptide mapping, taking into account the mechanism of bromouracil mutagenesis.

The effect of the amino acid substitution is discussed: A direct relationship exists between structural alteration, increased energy of activation of lysozyme reaction and elevated minimal temperature of growth of the cs-mutant compared to that of the wild type.

This is a preview of subscription content, log in to check access.

Literature

  1. Artemev, M. I., Ravin, V. K.: Fine structure of lysozyme gene of bacteriophage T4B. Genetika 9 (8), 123 (1973)

  2. Atissa, M. Z., Habeeb, A. F. S. A.: Enzymatic and immunochemical properties of lysozyme. I. Derivatives modified at tyrosine. Influence of nature of modification on activity. Biochemistry 8, 1385 (1969)

  3. Babel, W., Rosenthal, H. A., Rapoport, S.: A unified hypothesis on the causes of cardinal temperatures of microorganisms; the temperature minimum of Bacillus stearothermophilus. Acta biol. med. germ. 28, 565 (1972)

  4. Boyer, S. H., Crosby, E. F., Noyes, A. N., Fuller, G. F., Leslie, S. E., Donaldson, L. J., Vrablik, G. R., Schaefer, E. W., Thurmon, T. F.: Primate haemoglobins: some sequences and some proposals concerning the character of evolution and mutation. Biochem. Genet. 5, 405 (1971)

  5. Bratu, V., Lorkin, P. A., Lehmann, H., Predescu, C.: Haemoglobin Bucuresti β42(CDI) Phe → Leu, a cause of unstable haemoglobin haemolytic anaemia. Biochim. biophys. Acta (Amst.) 251, 1 (1971)

  6. Canfield, R. E.: Peptides derived from tryptic digestions of egg-white lysozyme. J. biol. Chem. 238, 2691 (1963)

  7. Carrell, R. W., Lehmann, H., Hutchinson, H. E.: Haemoglobin Köln (β98 Val → Met): an unstable protein causing inclusion-body anaemia. Nature (Lond.) 210, 915 (1966)

  8. Dauberschmidt, R., Liebscher, D.-H.: Über eine kälteempfindliche (cs-) Mutante im Lysozymgen des Bakteriophagen T4. Dissertation der Medizinischen Fakultät der Humboldt-Universität, Berlin 1973

  9. Dauberschmidt, R., Liebscher, D.-H., Thiele, B.-J., Rapoport, S. M., Heitmann, P., Rosenthal, H. A.: Untersuchungen über Phagenlysozym. III. Reinigung und vergleichende Charakterisierung des Lysozyms des T4D-Wildtyps und der kälteempfindlichen Mutante cseBU56. Acta biol. med. germ. 32, 315 (1974)

  10. Dayhoff, M. O., Eck, R. V.: Atlas of protein sequence and structure 1967–1968. Silver Spring 1968

  11. Dreyer, W. J.: Conference on molecular and radiation biology. Nat. Acad. Sci. Publ. (Wash.) 823, 129 (1961)

  12. Dunnill, P.: Sequence similarities between hen egg-white and T4 phage lysozyme. Nature (Lond.) 215, 621 (1967)

  13. Easley, C. W.: Combinations of specific colour reactions useful in the peptide mapping. Biochim. biophys. Acta (Amst.) 107, 388 (1965)

  14. Edelhoch, H.: Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948 (1967)

  15. Epstein, C. J., Goldberger, R. F.: A study of factors influencing the reactivation of reduced egg-white lysozyme. J. biol. Chem. 238, 1380 (1963)

  16. Freese, E.: Molecular mechanism of mutations. In: Molecular genetics I (ed. Taylor, H. J.), p. 207. New York-London: Acad. Press 1963

  17. Imada, M., Inouye, M., Eda, M., Tsugita, A.: Frameshift mutation in the lysozyme gene of bacteriophage T4: demonstration of the insertion of four bases and the preferential occurrence of base addition in acridine mutagenesis. J. molec. Biol. 54, 199 (1970)

  18. Ingram, V. M., Stretton, A. O. W.: Human haemoglobln A2. I. Comparison of haemoglobins A2 and A. Biochim. biophys. Acta (Amst.) 62, 456 (1962)

  19. Inouye, M., Okada, Y., Tsugita, A.: The amino acid sequence of T4 phage lysozyme. I. Tryptic digestion. J. biol. Chem. 245, 3439 (1970)

  20. Inouye, M., Tsugita, A.: The amino acid sequence of T4 bacteriophage lysozyme. J. molec. Biol. 22, 193 (1966)

  21. Katz, A. M., Dreyer, W. J., Anfinsen, C. B.: Peptide separation by two-dimensional chromatography and electrophoresis. J. biol. Chem. 234, 2897 (1959)

  22. Kravchenko, N. A., Lapuk, V. K.: The route of the selective tryptophan photooxidation in lysozyme. Biokhimiya 35, 64 (1970)

  23. Liebscher, D.-H., Dauberschmidt, R., Rosenthal, H. A.: Untersuchungen über Phagenlysozym. I. Isolierung und erste biochemische Charakterisierung einer T4Dcs-Lysozymmutante. Acta biol. med. germ. 26, K 1 (1971)

  24. Liebscher, D. H., Dauberschmidt, R., Rosenthal, H. A.: Untersuchungen über Phagenlysozym. II. Isolierung und Charakterisierung von kälteempfindlichen Mutanten im Lysozymgen des Phagen T4. Z. allg. Mikrobiol. 14, 395 (1974)

  25. Okada, Y., Amagase, S., Tsugita, A.: Frameshift mutation in the lysozyme gene of bacteriophage T4: demonstration of the insertion of five bases, and a summary of in vivo codons and lysozyme activities. J. molec. Biol. 54, 219 (1970)

  26. Parson, S. M., Jao, L., Dahlquist, F. W., Borders, C. L., Graff, T., Racs, J., Raftery, M. A.: The nature of amino acid side chains which are critical for the activity of lysozyme. Biochemistry 8, 700 (1969)

  27. Pataki, G.: Dünnschichtchromatographie in der Aminosäure- und Peptidchemie. Berlin: Walter de Gruyter & Co. 1966

  28. Phillips, D. C.: The hen egg-white lysozyme molecule. Proc. nat. Acad. Sci. (Wash.) 57, 484 (1967)

  29. Schachner, M., Zillig, W.: Fingerprint maps of tryptic peptides from subunits of Escherichia coli and T4-modified DNA-dependent RNA polymerase. Europ. J. Biochem. 22, 513 (1971)

  30. Stahl, E.: Dünnschichtchromatographie. Berlin-Göttingen-Heidelberg: Springer 1966

  31. Tsugita, A., Inouye, M.: Complete primary structure of phage lysozyme from Escherichia coli T4. J. molec. Biol. 37, 201 (1968)

  32. Tsugita, A., Inouye, M., Terzaghi, E., Streisinger, G.: Purification of bacteriophage T4 lysozyme. J. biol. Chem. 243, 391 (1968)

  33. Udenfriend, S.: Fluorescence assay in biology and medicine. New York-London: Acad. Press 1962

  34. Wieland, T., Pfleiderer, G.: Analytische und mikropräparative Trägerelektrophorese mit höheren Spannungen. Angew. Chem. 67, 257 (1955)

Download references

Author information

Additional information

Vorgelegt von H. Böhme

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Liebscher, D.-., Dauberschmidt, R., Rapoport, S.M. et al. Untersuchungen über Phagenlysozym. Molec. Gen. Genet. 132, 321–333 (1974). https://doi.org/10.1007/BF00268572

Download citation