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

Kazuho Ikeo*, Kei Takahashi, Takashi Gojobori

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)331-336
Number of pages6
JournalJournal of Molecular Evolution
Volume40
Issue number3
DOIs
StatePublished - 1995
Externally publishedYes

Keywords

  • Domain evolution
  • Kringle domain
  • Protease domain
  • Serine protease

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Genetics

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