Evolutionary Studies on Teleost Hemoglobin
Sequences
Wytze T. Stam\ Jaap J. Beintema 2 , Rossana D' Avino 3 ,
Maurizio Tamburrini 3 , Ennio Cocca 3 , and Guido di Prisco 3
IDepartment of Marine Biology
2Department of Biochemistry, University of Groningen, Kerklaan 30,9751
NN Haren, The Netherlands
3Institute of Protein Biochemistry and Enzymology, CNR, Naples, Italy
Introduction
During cold adaptation, the blood of Antarctic fish has acquired some
features which clearly differentiate these fish from fish of temperate and
tropical climates. A much lower erythrocyte and hemoglobin content
counteracts the temperature-induced viscosity increase in the blood and,
consequently, cardiac work is greatly facilitated. At the extreme end of
such evolution, the blood of the Notothenioid family Channichthyidae
(a unique case among vertebrates) is characterized by the total lack of
hemoglobin.
We have initiated investigations on the relationship between the
molecular structure and the biological function in hemoglobins of
Antarctic teleosts belonging to the suborder Notothenioidei.
Hemolysates of these fish species generally contain a single major
hemoglobin and often a second minor component (about 5% of the
total). The markedly reduced hemoglobin multiplicity of Antarctic fish
in comparison with teleosts living in temperate and tropical waters may
be expected, since hemoglobin multiplicity is likely to be linked with
the variability of the environment [1], and the Antarctic waters are a
stable habitat.
In a previous paper [2] amino acid sequences of a,- and ~-chains of
human hemoglobin, and of hemoglobins of coelacanth and 24 teleost
fish species, including 13 Notothenioidei, were analyzed using
maximum parsimony. Trees were derived for the a,- and ~-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 a,- and ~-chains were highly congruent, and indicated a
specific pattern of gene duplications and gene expression of teleost
hemoglobins which has not yet been analyzed at the genomic level.
G. di Prisco, E. Pisano, A. Clarke (Eds)
Fishes of Antarctica. A biological overview
© Springer-Verlag Italia 1998
Sequences
Wytze T. Stam\ Jaap J. Beintema 2 , Rossana D' Avino 3 ,
Maurizio Tamburrini 3 , Ennio Cocca 3 , and Guido di Prisco 3
IDepartment of Marine Biology
2Department of Biochemistry, University of Groningen, Kerklaan 30,9751
NN Haren, The Netherlands
3Institute of Protein Biochemistry and Enzymology, CNR, Naples, Italy
Introduction
During cold adaptation, the blood of Antarctic fish has acquired some
features which clearly differentiate these fish from fish of temperate and
tropical climates. A much lower erythrocyte and hemoglobin content
counteracts the temperature-induced viscosity increase in the blood and,
consequently, cardiac work is greatly facilitated. At the extreme end of
such evolution, the blood of the Notothenioid family Channichthyidae
(a unique case among vertebrates) is characterized by the total lack of
hemoglobin.
We have initiated investigations on the relationship between the
molecular structure and the biological function in hemoglobins of
Antarctic teleosts belonging to the suborder Notothenioidei.
Hemolysates of these fish species generally contain a single major
hemoglobin and often a second minor component (about 5% of the
total). The markedly reduced hemoglobin multiplicity of Antarctic fish
in comparison with teleosts living in temperate and tropical waters may
be expected, since hemoglobin multiplicity is likely to be linked with
the variability of the environment [1], and the Antarctic waters are a
stable habitat.
In a previous paper [2] amino acid sequences of a,- and ~-chains of
human hemoglobin, and of hemoglobins of coelacanth and 24 teleost
fish species, including 13 Notothenioidei, were analyzed using
maximum parsimony. Trees were derived for the a,- and ~-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 a,- and ~-chains were highly congruent, and indicated a
specific pattern of gene duplications and gene expression of teleost
hemoglobins which has not yet been analyzed at the genomic level.
G. di Prisco, E. Pisano, A. Clarke (Eds)
Fishes of Antarctica. A biological overview
© Springer-Verlag Italia 1998
