Journal of Molecular Evolution

, Volume 13, Issue 1, pp 57–72 | Cite as

Evolutionary changes in protein composition — evidence for an optimal strategy

  • R. Coutelle
  • G. L. Hofacker
  • R. D. Levine
Article

Summary

The information contained in the composition of different proteins of the same family is analyzed. It is found that within each family the gain in information per amino acid replacement is constant. This finding is interpreted to imply that evolutionary changes in proteins follow an “optimal” path in the sense that they maximize the number of potentially functional sequences that can be generated by T accepted point mutations from a given protein, subject to restrictions due to biological function.

Key words

Information gain by accepted point mutations Protein evolution Protein compositions 

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References

  1. Ben-Shaul, A., Hofacker, G.L. (1976). Statistical and Dynamical Models of Population Inversion. In: Handbook of Chemical Lasers, R.W.F. Gross and J.F. Bott, eds., pp. 579–617. New York: WileyGoogle Scholar
  2. Berg, A. van den, Beintema, J.J. (1975). Nature253, 207–210Google Scholar
  3. Berg, A. van den, Hende-Timmer, L. van den, Beintema, J.J. (1976). BBA453, 400–409Google Scholar
  4. Berg, A. van den, Hende-Timmer, L. van den, Hofsteenge, J., Gaastra, W., Beintema, J.J. (1977). Eur. J. Biochem.75, 91–100Google Scholar
  5. Bogardt, R.A., Dwulet, F.E., Lehman, L.D., Jones, B.N., Gurd, F.R.N. (1976). Biochemistry15, 2597–2602Google Scholar
  6. Castillo, O., Lehmann, H. (1977). BBA492, 232–236Google Scholar
  7. Chirpich, T.P. (1975). Science188, 1022–1023Google Scholar
  8. Dayhoff, M.O., Dayhoff, R.E., Hunt, L.T. (1976). Compositions of Proteins. In: Atlas of Protein Sequence and Structure, M.O. Dayhoff, ed., Vol. 5, Suppl. 2, p. 301. Silver Spring, Maryland: National Biomedical Research SocietyGoogle Scholar
  9. Dayhoff, M.O., Eck, E.V., Park, C.M. (1972). A Model of Evolutionary Change in Proteins. In: Atlas of Protein Sequence and Structure, M.O. Dayhoff, ed., Vol. 5, pp. 89–99. Silver Spring, Maryland: National Biomedical Research FoundationGoogle Scholar
  10. Deconinck, M., Peiffer, S., Depreter, J., Paul, C., Schnek, A.G., Leonis, J. (1975). BBA386, 567–575Google Scholar
  11. Dumur, V., Dautrevaux, M., Han, K. (1976). BBA427, 759–761Google Scholar
  12. Dwulet, F.E., Bogardt, R.A., Jones, B.N., Lehman, L.D. (1975). Biochemistry14, 5336–5443Google Scholar
  13. Dwulet, F.E., Jones, B.N., Lehman, L.D., Gurd, F.R.N. (1977). Biochemistry16, 873–876Google Scholar
  14. Emmens, M., Welling, G.W., Beintema, J.J. (1976). Biochem. J.157, 317–323Google Scholar
  15. Finkelstein, A.V., Ptitsyn, O.B. (1971). J. Mol. Biol.62, 613–624Google Scholar
  16. Gatlin, L.L. (1972). Information Theory and the Living System, New York: Columbia Univ. PressGoogle Scholar
  17. Gatlin, L.L. (1974). J. Mol. Evol.3, 189–208Google Scholar
  18. Gatlin, L.L. (1976). J. Mol. Evol.7, 185–195Google Scholar
  19. Groen, G., Welling, G.W. Beintema, J.J. (1975). FEBS Lett.60, 300–304Google Scholar
  20. Hartley, R.V. (1928). Bell System Techn. J.7, 535–563Google Scholar
  21. Hase, T., Ohmiya, M., Matsubara, H., Mullinger, R.N., Rao, K.K., Hall, D.O. (1976a). Biochem. J.159, 55–63Google Scholar
  22. Hase, T., Wada, K., Ohmiya, M., Matsubara, H., (1976b). J. Biochem.80, 993–999Google Scholar
  23. Hase, T., Wakabayshi, S., Matsubara, H., Kerscher, L., Oesterhelt, D., Rao, K.K., Hall, D.O. (1977). FEBS Lett.77, 308–310Google Scholar
  24. Hasegawa, M., Yano, T.A. (1975). Origins of Life6, 219–227Google Scholar
  25. Hermann, J., Jollés, J., Buss, D.H., Jollés, P. (1973). J. Mol. Biol.79, 587–595Google Scholar
  26. Holmquist, R. (1975). J. Mol. Evol.4, 277–306Google Scholar
  27. Holmquist, R., Moise, H. (1975). J. Mol. Evol.6, 1–14Google Scholar
  28. Hopfinger, A.J. (1972). Currents in Mod. Biol. Biosystems5, 38–42Google Scholar
  29. Jollés, J., Schoentgen, F., Jollés, P., Prager, E.M., Wilson, A.C. (1976). J. Mol. Evol.8, 59–78Google Scholar
  30. Jones, B.N., Vigna, R.A., Dwulet, F.E., Bogardt, R.A., Lehman, L.D., Gurd, F.R.N. (1976). Biochemistry15, 4418–4422Google Scholar
  31. Jong, W.W. de, Gleaves, J.T., Boulter, D. (1977). J. Mol. Evol.10, 123–135Google Scholar
  32. Kimura, M. (1968). Nature217, 624–626Google Scholar
  33. King, J.L., Jukes, T.H. (1969). Science164, 788–798Google Scholar
  34. Kullback, S. (1959). Information Theory and Statistics, New York: WileyGoogle Scholar
  35. Lehman, L.D., Dwulet, F.E., Bogardt, R.A., Jones, B.N., Gurd, F.R.N. (1977). Biochemistry16, 706–709Google Scholar
  36. Levine, R.D., Ben-Shaul, A. (1977). In: Chemical and Biochemical Applications of Lasers, C.B. Moore, ed., Vol. II, pp. 145–197, London: Academic PressGoogle Scholar
  37. Levine, R.D., Bernstein, R.B. (1974). Accts. Chem. Res.7, 393–400Google Scholar
  38. Lin, K.D., Kim, V.K., Chernoff, A.J. (1976). Biochem. Genet.14, 427–440Google Scholar
  39. Lyddiat, A., Boulter, D. (1976a). FEBS Lett.62, 85–88Google Scholar
  40. Lyddiat, A., Boulter, D. (1976b). FEBS Lett.67, 331–334Google Scholar
  41. Lyddiat, A., Boulter, D. (1977). Biochem. J.163, 333–338Google Scholar
  42. Martinez, G., Rochat, H., Ducet, G. (1974). FEBS Lett.47, 212–217Google Scholar
  43. Matsuda, G., Maita, T., Watanabe, B., Araya, A., Morokuma, K., Goodman, M., Prychodko, W. (1973). Hoppe-Seyler's Z. Physiol. Chem.354, 1153–1155Google Scholar
  44. Nagano, K. (1973). J. Mol. Biol.75, 401–420Google Scholar
  45. Ohta, T., Kimura, M. (1971a). J. Mol. Evol.1, 18–25Google Scholar
  46. Ohta, T., Kimura, M. (1971b). Science174, 150–153Google Scholar
  47. Reichert, T.A., Cohen, D.N., Wong, A.K.C. (1973). J. Theor. Biol.42, 245–261Google Scholar
  48. Renyi, A. (1962). Wahrscheinlichkeitsrechnung. Berlin-Ost: Deutscher Verlag der Wissenschaften (in English 1970: Probability Theory, Amsterdam: North-Holland)Google Scholar
  49. Romero-Herrera, A.E., Lehmann, H. (1974). BBA359, 236–241Google Scholar
  50. Romero-Herrera, A.E., Lehmann, H., Fakes, W. (1975a). BBA379, 13–21Google Scholar
  51. Romero-Herrera, A.E., Lehmann, H. (1975b), BBA393, 205–214Google Scholar
  52. Romero-Herrera, A.E., Lehmann, H. (1975c). BBA400, 387–398Google Scholar
  53. Romero-Herrera, A.E., Lehmann, H., Castillo, O. (1976a). BBA420, 387–396Google Scholar
  54. Romero-Herrera, A.E., Lehmann, H., Castillo, O. (1976b). BBA439, 51–54Google Scholar
  55. Rousseaux, J., Dautrevaux, M., Han, K. (1976). BBA439, 55–62Google Scholar
  56. Schlögl, F. (1975). Z. PhysikB 20, 177–184Google Scholar
  57. Shannon, C.E., Weaver, W. (1949). The Mathematical Theory of Communication, Univ. of Illinois Press, UrbanaGoogle Scholar
  58. Smith, T.F. (1969). Math. Biosciences4, 179–187Google Scholar
  59. Stenzel, P. (1974). Nature252, 62–63Google Scholar
  60. Takei, H., Ota, Y., Wu, K.C., Kiyohara, T., Matsuda, G. (1975). J. Biochem.77, 1345–1347Google Scholar
  61. Tanaka, M., Haniu, M., Yasunobu, K.T., Evans, M.C.W., Rao, K.K. (1975). Biochemistry14, 1938–1943Google Scholar
  62. Tentori, L., Vivaldi, G., Carta, S., Marinucci, M., Massa, A., Antonini, N.E., Brunori, M. (1973). I.J. Pept. Prot. Res.5, 187–200Google Scholar
  63. Vogel, H. (1975). J. Mol. Evol.6, 271–283Google Scholar
  64. Vogel, H. Zuckerkandl, E. (1971). In: Molecular Evolution, E. Schofeniels, ed., Vol. II, pp. 352–365Google Scholar
  65. Wada, K., Hase, T., Tokunaga, H., Matsubara, H. (1975). FEBS Lett.55, 102–104Google Scholar
  66. Welling, G.W., Groen, G., Beintema, J.J. (1975). Biochem. J.147, 505–511Google Scholar

Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • R. Coutelle
    • 1
  • G. L. Hofacker
    • 1
  • R. D. Levine
    • 2
  1. 1.Lehrstuhl für Theoretische ChemieTechnische Universität MünchenGarchingFederal Republic of Germany
  2. 2.Department of Physical ChemistryThe Hebrew UniversityJerusalemIsrael

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