Molecular evolution of hemoglobins of Antarctic fishes (Notothenioidei)

W.T. Stam, J.J Beintema, R. D Avino, M. Tamburrini, G. di Prisco

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Abstract

Amino acid sequences of alpha- and beta-chains of human hemoglobin and of hemoglobins of coelacanth and 24 teleost fish species, including 11 antarctic and two temperate Notothenioidei, were analyzed using maximum parsimony. Trees were derived for the alpha- and beta-chains separately and for tandemly arranged sequences, using the human and coelacanth sequences as outgroups in all analyses. The topologies of the trees of the alpha- and beta-chains are highly congruent and indicate a specific pattern of gene duplications and gene expression of teleost hemoglobins which has not yet been investigated into more detail. The Notothenioid fish generally contain a single major hemoglobin and often a second minor component. The alpha- and beta-chains of the major components form a monophyletic group in all investigated trees, with the nonantarctic Pseudaphritis as their sister taxon. The minor chains also are a monophyletic group and form an unresolved cluster with the major chains and the hemoglobins of tuna and red gurnard. The Notothenioid families Nototheniidae and Bathydraconidae appear to be paraphyletic.

Original languageEnglish
Pages (from-to)437-445
Number of pages9
JournalJournal of Molecular Evolution
Volume45
Issue number4
Publication statusPublished - Oct-1997

Keywords

  • Antarctica
  • cold-adapted teleosts
  • hemoglobin
  • most parsimonious tree
  • Notothenioidei
  • AMINO-ACID-SEQUENCE
  • OXYGEN-BINDING PROPERTIES
  • SINGLE HEMOGLOBIN
  • ALPHA-GLOBIN
  • TELEOST
  • MITOCHONDRIAL
  • PERCIFORMES
  • EQUILIBRIA
  • COMPONENTS
  • FAMILY

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