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The phylogeny of polar fishes and the structure, function and molecular evolution of hemoglobin

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Abstract

Fishes thriving in polar habitats offer many opportunities for comparative approaches to understanding protein thermal adaptations. Investigations on the remarkable evolutionary adaptations to these environments of basic proteins such as hemoglobin, the oxygen carrier, can provide new insights into the mechanisms studied in temperate organisms and can shed light on convergent processes evolved in response to thermal adaptations. At the molecular level, hemoglobins are one of the most intriguing systems for studying the relationships between environmental conditions and adaptations. This review summarizes the current knowledge on molecular structure, biological function and phylogeny of hemoglobins of fish species living in both polar habitats but having different evolutionary histories. In benthic, non-migratory, cold-adapted fishes, the stability of thermal conditions may have generated no or few variations in selective pressures on globin sequences through evolutionary time, so that sequences retain the species phylogenetic “signal”. In pelagic, migratory, cold-adapted or temperate fishes, variations in selective pressures on globin sequences caused by variations in temperature accompanying the dynamic life style may have disrupted the phylogenetic “signal” in phenetic trees.

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Acknowledgments

We thank Professor Dr. G. Hempel for inviting us to write this review. This study is supported by the Italian National Programme for Antarctic Research (PNRA). It is in the framework of the Arctic Strategic Programme of the Italian National Research Council, the SCAR programmes Ecology of the Antarctic Sea Ice Zone (EASIZ), Evolutionary Biology of Antarctic Organisms (EVOLANTA) and Evolution and Biodiversity in the Antarctic (EBA), and the 2003 and 2005 TUNU-I and TUNU-II cruises near Greenland. We also thank the captain, crew and personnel of Raytheon Polar Services aboard the RVIB Nathaniel B. Palmer for their excellent assistance during the ICEFISH cruise. The ICEFISH cruise was supported by National Science Foundation grant OPP 01-32032 to H. William Detrich (Northeastern University, Boston USA).

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  1. Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, Naples, 80131, Italy

    Cinzia Verde & Guido di Prisco

  2. Département Systématique et Evolution, Muséum National d’Histoire Naturelle, UMR 7138 CNRS, CP26, 57, rue Cuvier, Paris, 75005, France

    Guillaume Lecointre

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  1. Cinzia Verde
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  2. Guillaume Lecointre
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Correspondence to Guido di Prisco.

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Verde, C., Lecointre, G. & di Prisco, G. The phylogeny of polar fishes and the structure, function and molecular evolution of hemoglobin. Polar Biol 30, 523–539 (2007). https://doi.org/10.1007/s00300-006-0217-3

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