Molecular evolution of hemoglobins of antarctic fishes (Notothenioidei) |
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Authors: | Wytze T Stam Jaap J Beintema Rossana D’Avino Maurizio Tamburrini Guido di Prisco |
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Institution: | (1) Department of Marine Biology, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands, NL;(2) Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands, NL;(3) Institute of Protein Biochemistry and Enzymology, C.N.R., Via Marconi 10, 80125 Naples, Italy, IT |
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Abstract: | Amino acid sequences of α- and β-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
α- and β-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 α-and β-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 α- and β-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.
Received: 26 March 1997 / Accepted: 7 May 1997 |
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Keywords: | : Antarctica — Cold-adapted teleosts — Hemoglobin — Most parsimonious tree — Notothenioidei |
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