Skip to main content

The Creation of a New Gene from a Redundant Duplicate of an Old Gene

  • Chapter
Evolution by Gene Duplication

Abstract

The type of gene duplication which produced the group of isozyme genes contributed greatly to the evolution of increasingly complex organisms. These functionally diverged duplicated genes, however, still specify the same enzyme in that their products act upon the same substrate with the help of the same coenzyme. A, B and C-subunits of LDH of any vertebrate must still maintain either the identical active site sequence of 12 amino acids (— Val-Ile-Ser-Gly-Gly-Cys-Asn-Leu-Asp-Thr-Ala-Arg —), or a sequence very similar to the above, for this is the sequence which binds with NAD and recognizes pyruvate or lactate as the substrate (Kaplan, 1965). Differences in the kinetic property of A, B and C-subunits must reflect amino acid substitutions which affect sites other than the active site of the polypeptide chain.

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

Access this chapter

eBook
USD 16.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 119.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Baglioni, C.: Homologies in the position of cysteine residues of K and L type chains of human immunoglobins. Biochem. Biophys. Res. Commun. 26, 82–89 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Black, J.A., Dixon, G.H.: Amino-acid sequence of alpha chain of human haptoglobins. Nature 218, 736–741 (1968).

    Article  PubMed  CAS  Google Scholar 

  • Borisy, G.G., Taylor, E.W.: The mechanism of action of colchicine: binding of colchicine-3H to cellular protein. J. Cell Biol. 34, 523–533 (1967).

    Google Scholar 

  • Burnet, F.M.: The clonal selection theory of acquired immunity. London: Cambridge Univ. Press 1958.

    Google Scholar 

  • Doolittle, R.F., Singer, S.J., Metzger, H.: Evolution of immunoglobulin polypeptide chains: Carboxyterminal of an IgM heavy chain. Science 154, 1561–1562 (1966).

    Article  PubMed  CAS  Google Scholar 

  • Edmundson, A.B.: Amino-acid sequence of sperm whale myoglobin. Nature 205, 883–887 (1965).

    Article  CAS  Google Scholar 

  • Eigsti, O.J., Dustin, P., Jr.: Colchicine in agriculture, medicine, biology and chemistry. Ames (Iowa): Iowa State College Press 1955.

    Google Scholar 

  • Glick, B., Chang, T.S., Jaap, R.G.: The bursa of Fabricius and antibody production. Poultry Sci. 35, 224–234 (1956).

    Article  Google Scholar 

  • Gray, W., Dreyer, W., Hood, L.: Mechanism of antibody synthesis: Size difference between mouse kappa chains. Science 155, 465–467 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Hildemann, W.H., Thoenes, G.H.: Immunological response of Pacific hagfish. I. Skin transplantation immunity. Transplantation 7, 506–529 (1969).

    CAS  Google Scholar 

  • Hilschmann, N., Craig, L.C.: Amino acid sequence studies with Bence-Jones proteins. Proc. Natl. Acad. Sci. US 53, 1403–1409 (1965).

    Article  CAS  Google Scholar 

  • Hilse, K., Sorger, U., Braunitzer, G.: Zur Phylogenie des Hämoglobinmoleküls über den Polymorphismus und die N-terminalen Aminosäuren des Karpfenhämoglobins. Z. physiol. Chem., Hoppe Seyler’s 344, 166–168 (1966).

    Article  CAS  Google Scholar 

  • Ingram, V.M.: The hemoglobin in genetics and evolution. New York: Columbia University Press 1963.

    Google Scholar 

  • Kaplan, N.O.: Evolution of dehydrogenases. In: Evolving genes and proteins (Bryson, W., Vogel, H.J., Eds.). New York: Academic Press 1965.

    Google Scholar 

  • Kauffman, D.L.: The disulphide bridges of trypsin. J. Mol. Biol. 12, 929–932 (1965).

    Article  PubMed  CAS  Google Scholar 

  • Keil, B., Prusik, Z., Šorm, F.: Disulphide bridges and a suggested structure of chymotrypsinogen. Biochim. et Biophys. Acta 78, 559–561 (1963).

    Article  CAS  Google Scholar 

  • Kendrew, J.C., Dickerson, R.E., Strandberg, B.E., Hart, R.G., Davies, D.R., Phillips, D.C., Shore, U.C.: Structure of myoglobin: A three-dimensional fourier synthesis at 2Å resolution obtained by X-ray analysis. Nature 185, 422–427 (1960).

    Article  PubMed  CAS  Google Scholar 

  • Lennox, E., Cohn, M.: Immunoglobin genetics. Ann. Rev. Biochem. 36, 365–406 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Marchalonis, J., Edelman, G.M.: (1) Polypeptide chains of immunoglobulins from the smooth dogfish (Mustelus canis). Science 154, 1567–1568 (1966).

    Article  PubMed  CAS  Google Scholar 

  • — (2) Phylogenetic origins of antibody structure. II. Immunoglobulins in the primary immune response of the bullfrog, Rana catesbiana. J. Exptl. Med. 124, 901–913 (1966).

    Article  CAS  Google Scholar 

  • Margoliash, E.: Primary structure and evolution of cytochrome C. Proc. Natl. Acad. Sci. US 50, 672–679 (1963).

    Article  CAS  Google Scholar 

  • Miller, J.F.A.P.: Immunological function of the thymus. Lancet 1961 II, 748–749.

    Article  Google Scholar 

  • Milstein, C.: The disulphide bridges of immunoglobulin ϰ-chains. Biochem. J. 101, 338–351 (1966).

    PubMed  CAS  Google Scholar 

  • Neurath, H., Walsh, K.A., Winter, W.P.: Evolution of structure and function of proteases. Science 158, 1638–1644 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Ohno, S., Morrison, M.: Multiple gene loci for the monomeric hemoglobin of the hagfish (Eptatretus stoutii). Science 154, 1034–1035 (1966)

    Article  PubMed  CAS  Google Scholar 

  • Okazaki, K., Holtzer, H.: Aspects of myogenesis in vitro. J. Cell Biol. 27, 75A (1965).

    Google Scholar 

  • Papermaster, B.W., Condie, R.M., Finstad, J., Good, R.A.: Immune response in the California hagfish. Nature 196, 355–356 (1962).

    Article  PubMed  CAS  Google Scholar 

  • Perutz, M.F., Rossmann, M.B., Cullis, A.F., Muirhead, H., Will, G., North, A.C.T.: Structure of hemoglobin: A three dimensional fourier synthesis at 5.5 Å resolution, obtained by X-ray analysis. Nature 185, 416–422 (1960).

    Article  PubMed  CAS  Google Scholar 

  • Porter, R.R.: A discussion of the chemistry and biology of immunoglobulins. Proc. Roy. Soc. (London), B 166, 113–243 (1966).

    Google Scholar 

  • Renaud, F.L., Rowe, A.J., Gibbons, I.R.: Some properties of the protein forming the outer fibers of cilia. J. Cell Biol. 36, 79–90 (1968).

    Article  CAS  Google Scholar 

  • Rudloff, V., Zelenik, M., Braunitzer, G.: Zur Phylogenie des Hämoglobinmoleküls, Untersuchungen am Hämoglobin des Flußneunauges (Lampetra fluviatilis). Z. physiol. Chem., Hoppe Seyler’s 344, 284–288 (1966).

    Article  CAS  Google Scholar 

  • Shelansky, M.L., Taylor, E.W.: Properties of the protein subunit of central-pair and outer-doublet microtubulues of sea urchin flagella. J. Cell Biol. 38, 304–315 (1968).

    Article  Google Scholar 

  • Szent-Györgyi, A.: Chemistry of muscular contraction. New York: Academic Press 1957.

    Google Scholar 

  • Tilney, L.G., Hiramoto, Y., Marsland, G.: Studies on the microtubules in heliozoa. III. A pressure analysis of the role of these structures in the formation and maintenance of the axopidia of Actinosphaerium nucleofilum (Barrett). J. Cell Biol. 29, 77–95 (1966).

    Article  PubMed  CAS  Google Scholar 

  • Weisenberg, R.C., Borisy, G.G., Taylor, E.W.: The colchicine-binding protein of mammalian brain and its relation to microtubules. Biochem. J. 7, 4466–4479 (1968).

    Article  CAS  Google Scholar 

  • Wikler, M., Köhler, H., Shinoda, T., Putnam, F.W.: Macroglobulin structute: Homology of Mu and gamma heavy chains of human immunoglobulin. Science 163, 75–78 (1969).

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

Copyright information

© 1970 Springer Science+Business Media New York

About this chapter

Cite this chapter

Ohno, S. (1970). The Creation of a New Gene from a Redundant Duplicate of an Old Gene. In: Evolution by Gene Duplication. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-86659-3_14

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-86659-3_14

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-86661-6

  • Online ISBN: 978-3-642-86659-3

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics