Molecular adaptations in haemoglobins of notothenioid fishes.
Since haemoglobins of all animal species have the same haem group, differences in their properties, including oxygen affinity, electrophoretic mobility and pH sensitivity, must result from the interaction of the prosthetic group with specific amino-acid residues in the primary structure. For this reason, fish globins have been the subject of extensive studies in recent years, not only for their structural characteristics, but also because they offer the possibility to investigate the evolutionary history of these ancient molecules in marine and freshwater species living in a great variety of environmental conditions. This review summarizes the current knowledge on the structure, function and phylogeny of haemoglobins of notothenioid fishes. On the basis of crystallographic analysis, the evolution of the Root effect is analysed. Adaptation of the oxygen transport system in notothenioids seems to be based on evolutionary changes, involving levels of biological organization higher than the structure of haemoglobin. These include changes in the rate of haemoglobin synthesis or in regulation by allosteric effectors, which affect the amount of oxygen transported in blood. These factors are thought to be more important for short-term response to environmental challenges than previously believed.
Giordano
D
D
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy.
Russo
R
R
Coppola
D
D
di Prisco
G
G
Verde
C
C
D000222:Adaptation, Physiological / Q000502:physiology*; D000818:Animals; D004777:Environment; D019143:Evolution, Molecular; D006454:Hemoglobins / Q000378:metabolism*; D010473:Perciformes / Q000145:classification* / Q000378:metabolism / Q000502:physiology*; D010802:Phylogeny
D006454:Hemoglobins