caa a22 4500 467911835 CHVBK 20180406152851.0 cr unu---uuuuu 170328e20060801xx s 000 0 eng 10.1007/s11157-006-9001-7 doi (NATIONALLICENCE)springer-10.1007/s11157-006-9001-7 Molecular evolution of haemoglobins of polar fishes [Elektronische Daten] [Cinzia Verde, Daniela Giordano, Guido di Prisco] The Arctic and the Antarctic differ by age and isolation of the respective marine faunas. Antarctic fish are highly stenothermal, in response to stable water temperatures, whereas the Arctic ones are exposed to seasonal and latitudinal temperature variations. The knowledge of the mechanisms of phenotypic response to cold exposure in species of both polar habitats offers fundamental insights into the nature of environmental adaptation. In the process of cold adaptation, the evolutionary trend of Antarctic fish has led to unique specialisations, including modification of haematological characteristics, e.g. decreased amounts and multiplicity of haemoglobins. Unlike Antarctic Notothenioidei, Arctic teleosts have high haemoglobin multiplicity. Although the presence of functionally and structurally distinct haemoglobins is a plesiomorphic condition for many perciform-like fishes, it seems that the oxygen-transport system of teleost fish in the Arctic region has been adjusted to temperature differences and fluctuations of Arctic waters, much larger than in the Antarctic. The amino-acid sequences used to gain insight into the evolution history of α and β globins of polar fish have clearly shown that Antarctic and Arctic globins have different phylogenies, leading to the hypothesis that the selective pressure of environment stability allows the phylogenetic signal to be maintained in the Antarctic sequences, whereas environmental variability would tend to disrupt this signal in Arctic sequences. Springer Science+Business Media B.V., 2006 Antarctic nationallicence Arctic nationallicence Evolution nationallicence Fish nationallicence Globin gene nationallicence Haemoglobin nationallicence Verde Cinzia Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131, Naples, Italy aut Giordano Daniela Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131, Naples, Italy aut di Prisco Guido Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131, Naples, Italy aut Reviews in Environmental Science and Bio/Technology Kluwer Academic Publishers 5/2-3(2006-08-01), 297-308 1569-1705 5:2-3<297 2006 5 11157 https://doi.org/10.1007/s11157-006-9001-7 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11157-006-9001-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Verde Cinzia Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131, Naples, Italy aut NATIONALLICENCE 700 1- Giordano Daniela Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131, Naples, Italy aut NATIONALLICENCE 700 1- di Prisco Guido Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131, Naples, Italy aut NATIONALLICENCE 773 0- Reviews in Environmental Science and Bio/Technology Kluwer Academic Publishers 5/2-3(2006-08-01), 297-308 1569-1705 5:2-3<297 2006 5 11157 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer