The evolution of thermal adaptation in polar fish

Gene

Volumn 385, Issue , 2006, Pages 137-145

  Verde, Cinzia ^a   Parisi, Elio ^a   di Prisco, Guido ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Antarctica; Arctic; Bohr Root effect; Fish; Globin gene; Hemoglobin; Notothenioidei

Indexed keywords

HEMOGLOBIN;

ANTARCTICA; ARCTIC; BOHR EFFECT; CHEMICAL STRUCTURE; EVOLUTION; FISH; GLOBIN GENE; HISTORY; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; REVIEW; TEMPERATURE ACCLIMATIZATION;

ACCLIMATIZATION; ANIMALS; ANTARCTIC REGIONS; ARCTIC REGIONS; COLD CLIMATE; EVOLUTION; FISHES; GLOBINS; HEMOGLOBINS; PHYLOGENY; TEMPERATURE;

NOTOTHENIOIDEI; PISCES;

EID: 33845206135     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2006.04.006     Document Type: Review

References (54)

1. Balushkin A.V. Classification, phylogenetic relationships, and origins of the families of the suborder Notothenioidei (Perciformes). J. Ichthyol. 32 (1992) 90-110
2. Bargelloni L., Marcato S., Zane L., and Patarnello T. Mitochondrial phylogeny of notothenioids: a molecular approach to Antarctic fish evolution and biogeography. Syst. Biol. 49 (2000) 114-129
3. Berenbrink M., Koldkjær P., Kepp O., and Cossins A.R. Evolution of oxygen secretion in fishes and the emergence of a complex physiological system. Science 307 (2005) 1752-1757
4. Brey T., et al. Antarctic benthic diversity. Nature 368 (1994) 297
5. Brittain T. The Root effect. Comp. Biochem. Physiol. 86B (1987) 473-481
6. Bunn H.F. Differences in the interaction of 2,3-diphosphoglycerate with certain mammalian hemoglobins. Science 172 (1971) 1049-1052
7. Chen L., DeVries A.L., and Cheng C.-H.C. Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 3811-3816
8. Chen L., DeVries A.L., and Cheng C.-H.C. Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 3817-3822
9. Cheng C.-H.C. Evolution of the diverse antifreeze proteins. Curr. Opin. Genet. Dev. 8 (1998) 715-720
10. Clarke A., and Johnston I.A. Evolution and adaptive radiation of Antarctic fishes. TREE 11 (1996) 212-218
11. Cocca E., et al. Genomic remnants of alpha-globin genes in the hemoglobinless Antarctic icefishes. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 1817-1821
12. Cupane A., et al. Modification of alpha-chain or beta-chain heme pocket polarity by Val(E11)→Thr substitution has different effects on the steric, dynamic, and functional properties of human recombinant hemoglobin. Deoxy derivatives. J. Biol. Chem. 272 (1997) 26271-26278
13. D'Avino R., et al. Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. J. Biol. Chem. 269 (1994) 9675-9681
14. Dayton P.K., Mordida B.J., and Bacon F. Polar marine communities. Am. Zool. 34 (1994) 90-99
15. Dettaï A., and Lecointre G. Further support for the clades obtained by multiple molecular phylogenies in the acanthomorph bush. C. R. Biol. 328 (2005) 674-689
16. di Prisco G. Molecular adaptation of Antarctic fish hemoglobins. In: di Prisco G., Pisano E., and Clarke A. (Eds). Fishes of Antarctica. A Biological Overview (1998), Springer, Milano 339-353
17. di Prisco G., et al. The biochemistry of oxygen transport in red-blooded Antarctic fish. In: di Prisco G., Maresca B., and Tota B. (Eds). Biology of Antarctic Fish (1991), Springer-Verlag, Berlin 263-281
18. di Prisco G., Cocca E., Parker S.K., and Detrich H.W. Tracking the evolutionary loss of hemoglobin expression by the white-blooded Antarctic icefishes. Gene 295 (2002) 185-191
19. Eastman J.T. Ocular morphology in Antarctic notothenioid fishes. J. Morphol. 196 (1988) 927-934
20. Eastman J.T. Antarctic Fish Biology: Evolution in A Unique Environment (1993), Academic Press, San Diego, CA, USA
21. Eastman J.T. Comparison of the Antarctic and Arctic fish faunas. Cybium 12 (1997) 276-287
22. Eastman J.T. The nature of the diversity of Antarctic fishes. Polar Biol. 28 (2005) 93-107
23. Eastman J.T., and DeVries A.L. Renal glomerular evolution in Antarctic notothenioid fish. J. Fish Biol. 29 (1986) 649-662
24. Egginton S., Skilbeck C., Hoofd L., Calvo J., and Johnston I.A. Peripheral oxygen transport in skeletal muscle of Antarctic and sub-Antarctic notothenioid fish. J. Exp. Biol. 205 (2002) 769-779
25. Fairbanks M.B., Hoffert J.R., and Fromm P.O. The dependence of the oxygen concentrating mechanism of the teleost eye (Salmo gairdneri) on the enzyme carbonic anhydrase. J. Gen. Physiol. 54 (1969) 203-211
26. Farmer M., Fyhn H.J., Fyhn U.E.H., and Noble R.W. Occurrence of Root effect haemoglobins in Amazonian fishes. Comp. Biochem. Physiol. 62A (1979) 115-124
27. Giordano, D., Grassi, L., Parisi, E., Bargelloni, L., di Prisco, G., Verde, C., in press. Embryonic β-globin in the non-Antarctic nototthenioid fish Cottoperca gobio (Bovichtidae). Polar Biol.
28. e Sér 1 (1977) 67-74 (in French)
29. Ito N., Komiyama N.H., and Fermi G. Structure of deoxyhaemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded haemoglobin structures. J. Mol. Biol. 250 (1995) 648-658
30. Iwami T. Osteology and relationships of the family Channichthyidae. Mem. Natl. Inst. Polar Res., Tokyo, Ser. E Biol. Med. Sci. 36 (1985) 1-69
31. Kennett J.P. Cenozoic evolution of Antarctic glaciation, the Circum-Antarctic Ocean, and their impact on global paleoceanography. J. Geophys. Res. 82 (1977) 3843-3860
32. Lecointre G., Bonillo C., Ozouf-Costaz C., and Hureau J.-C. Molecular phylogeny of the Antarctic fishes: paraphyly of the Bovichitidae and no indication for the monophyly of the Notothenioidei (Teleostei). Polar Biol. 18 (1997) 193-208
33. Leinala E.K., Davies P.L., and Jia Z. Crystal structure of beta-helical antifreeze protein points to a general ice binding model. Structure 10 (2002) 619-627
34. Maruyama K., Yasumasu S., and Iuchi I. Evolution of globin genes of the medaka Oryzias latipes (Euteleostei; Beloniformes; Oryziinae). Mech. Dev. 121 (2004) 753-769
35. Mathews H.J., Rohlfs R.J., Olson J.S., Tame J., Renaud J.-P., and Nagai K. The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin. J. Biol. Chem. 264 (1989) 16573-16583
36. Mazzarella L., et al. Minimal structural requirements for root effect: crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi. Proteins 62 (2006) 316-321
37. Nagai K., et al. Distal residues in the oxygen binding site of haemoglobin studied by protein engineering. Nature 329 (1987) 858-860
38. Near T., Pesavento J.J., and Cheng C.-H.C. Phylogenetic investigations of Antarctic fishes (Perciformes: Notothenioidei) using complete gene sequences of the mitochondrial encoded 16S rRNA. Mol. Phylogenet. Evol. 32 (2004) 881-891
39. Pechick I., et al. Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)→threonine variant of hemoglobin. Biochemistry 35 (1996) 1935-1945
40. Perutz M.F. Species adaptation in a protein molecule. Mol. Biol. Evol. 1 (1983) 1-28
41. Perutz M.F., Fermi G., Luisi B., Shaanan B., and Liddington R. Stereochemistry of cooperativity mechanism in hemoglobin. Acad. Chem. Res. 20 (1987) 309-321
42. Pisano E., Ozouf-Costaz C., and Prirodina V. Chromosome diversification in Antarctic fish (Notothenioidei). In: di Prisco G., Pisano E., and Clarke A. (Eds). Fishes of Antarctica. A Biological Overview (1998), Springer, Milano 275-285
43. Riccio A., Tamburrini M., Carratore V., and di Prisco G. Functionally distinct hemoglobins of the cryopelagic Antarctic teleost Pagothenia borchgrevinki. J. Fish Biol. 57 (2000) 20-32
44. Riggs A. The Bohr effect. Annu. Rev. Physiol. 50 (1988) 181-204
45. Ruud J.T. Vertebrates without erythrocytes and blood pigment. Nature 173 (1954) 848-850
46. Stam W.T., Beintema J.J., D'Avino R., Tamburrini M., and di Prisco G. Molecular evolution of hemoglobins of Antarctic fishes (Notothenioidei). J. Mol. Evol. 45 (1997) 437-445
47. Tamburrini M., D'Avino R., Fago A., Carratore V., Kunzmann A., and di Prisco G. The unique hemoglobin system of Pleuragramma antarcticum, an Antarctic migratory teleost. Structure and function of the three components. J. Biol. Chem. 271 (1996) 23780-23785
48. Verde C., and di Prisco G. The oxygen transport system of polar fish: the evolution of hemoglobin. Ocean Polar Res. 25 (2003) 617-623
49. Verde C., Parisi E., and di Prisco G. The evolution of polar fish hemoglobin: a phylogenetic analysis of the ancestral amino acid residues linked to the Root effect. J. Mol. Evol. 57 (2003) S258-S267
50. Verde C., Carratore V., Riccio A., Tamburrini M., Parisi E., and di Prisco G. The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor. J. Biol. Chem. 277 (2002) 36312-36320
51. Verde C., et al. Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes. Protein Sci. 13 (2004) 2766-2781
52. Wittenberg J.B., and Wittenberg D.K. The choroid rete mirabile. I. Oxygen secretion and structure: comparison with the swimbladder rete mirabile. Biol. Bull. 146 (1974) 116-136
53. Yonetani T., Park S., Tsuneshige A., Imai K., and Kanaori K. Global allostery model of hemoglobin. J. Biol. Chem. 277 (2002) 34508-34520
54. Zhao Y., et al. The major adult α-globin gene of Antarctic teleosts and its remnants in the hemoglobinless icefishes: calibration of the mutational clock for nuclear genes. J. Biol. Chem. 273 (1998) 14745-14752