Skip to main content
Log in

Different evolutionary histories of kringle and protease domains in serine proteases: A typical example of domain evolution

Journal of Molecular Evolution Aims and scope Submit manuscript

Abstract

With the aim of elucidating the evolutionary processes of the kringle and protease domains in serine proteases which are involved with the system of blood coagulation and fibrinolysis, we constructed phylogenetic trees for the kringle and protease domains, separately, by use of amino acid sequence data. The phylogenetic trees constructed clearly showed that the topologies were different between the kringle and protease domains. Because both domains are coded by single peptides of serine proteases, this strongly suggests that the kringle and protease domains must have undergone different evolutionary processes. Thus, these observations imply that serine proteases evolve in a way such that each domain is a unit of evolution, exemplifying a typical mode of domain evolution. A possible relationship between the domain evolution and the exon shuffling theory is also discussed from the viewpoint of gene evolution.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

References

  • Doolittle RD, Bork P (1993) Evolutionary mobile modules in proteins. Scient Am Oct:50–56

  • Furie B, Furie CB (1988) The molecular basis of blood coagulation. Cell 53:505–518

    Google Scholar 

  • Gilbert W (1978) Why genes in pieces? Nature 271:501

    Google Scholar 

  • Gojobori T, Ishii K, Nei M (1982) Estimation of average number of nucleotide substitutions when the rate of substitution varies with nucleotide. J Mol Evol 18:414–423

    Google Scholar 

  • Gojobori T, Ikeo K (1994) Molecular evolution of serine protease and its inhibitor with special reference to domain evolution. Philos Trans R Soc Lond [B] 344:411–415

    Google Scholar 

  • Hein J (1990) A unified approach to alignments and phylogeny reconstruction. Methods Enzymol 183:626–645

    Google Scholar 

  • Holland SK, Blake CCF (1990) Proteins, exons, and molecular evolution. In: Stone EM, Schwartz RJ (eds) Intervening sequences in evolution and development. Oxford University Press, New York, pp 10–42

    Google Scholar 

  • Ikeo K, Takahashi K, Gojobori T (1991) Evolutionary origin of numerous Kringles in human and simian apolipoprotein(a). FEB S Lett 287:146–148

    Google Scholar 

  • Ikeo K, Takahashi K, Gojobori T (1992) Evolutionary origin of Kunitztype trypsin inhibitor domain inserted in the amyloid beta precursor protein of Alzheimer's disease. J Mol Evol 34:536–543

    Google Scholar 

  • Kimura M (1983) The neutral theory of molecular evolution. Cambridge University Press, Cambridge

    Google Scholar 

  • McLean JW, Tomlison JE, Kuang W-J, Eaton DL, Ellson YC, Fless GM, Scanu AM, Lawn RM (1987) cDNA sequence of human apolipoprotein(a) is homologous to plasminogen. Nature 330:132–137

    Google Scholar 

  • McMullen BA, Fujikawa K (1985) Amino acid sequence of the heavy chain of human a-factor XIIa (activated Hageman factor). J Biol Chem 260:5328–5341

    Google Scholar 

  • Miyazawa K, Tsubouchi H, Naka D, Takahashi K, Okigaki M, Arakaki N, Nakayama H, Hirono S, Sakiyama O, Takahashi K, Gohda E, Daikuhara Y, Kitamura N (1989) Molecular cloning and sequence analysis of cDNA for human hepatocyte growth factor. Biochem Biophys Res Commun 163:967–973

    Google Scholar 

  • Nakamura T, Nishizawa T, Hagiya M, Seki T, Shimonishi M, Sugimura A, Tashiro K, Shimizu S (1989) Molecular cloning and expression of human hepatocyte growth factor. Nature 342:440–443

    Google Scholar 

  • Needleman SB, Wunsch CD (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 48:443–453

    Google Scholar 

  • Nei M (1975) Molecular population genetics and evolution. NorthHolland, Amsterdam

    Google Scholar 

  • Neurath H (1984) Evolution of proteolytic enzymes. Science 224:350–357

    Google Scholar 

  • Patthy L (1985) Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 41:657–663

    Google Scholar 

  • Pennica D, Holmes WE, Kohr WJ, Harkins RN, Vehar GA, Bennet WM, Yelventon E, Seeburg PH, Heyneker L, Goeddel DV (1983) Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli. Nature 301:214–221

    Google Scholar 

  • Pesole G, Gerardi A, di Jeso F, Saccone C (1994) The peculiar evolution of apolipoprotein(a) in human and rhesus macaque. Genetics 136:255–260

    Google Scholar 

  • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Estimation of average number of nucleotide substitutions when the rate of substitution varies with nucleotide. Mol Biol Evol 4:406–425

    Google Scholar 

  • Sandra JFD, Ross T, MacGillivary A, Davie EW (1983) Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin. Biochemistry 22:2087–2097

    Google Scholar 

  • Schaller J, Moser PW, Dannegger-Muller GAK, Roselt SJ, Kampfer V, Rikli EE (1985) Complete amino acid sequence of bovine plasminogen comparison with human plasminogen. Eur J Biochem 149: 267–278

    Google Scholar 

  • Verde P, Stoppelli MP, Galeffi P, Nocera PD, Blasi F (1984) Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA. Proc Natl Acad Sci USA 81:4727–4731

    Google Scholar 

  • Walz DA, Hewett-Emmett D, Seegers WH (1977) Amino acid sequence of human prothrombin fragments 1 and 2. Proc Natl Acad Sci USA 74:1969–1972

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ikeo, K., Takahashi, K. & Gojobori, T. Different evolutionary histories of kringle and protease domains in serine proteases: A typical example of domain evolution. J Mol Evol 40, 331–336 (1995). https://doi.org/10.1007/BF00163238

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00163238

Key words

Navigation