Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus

Gene

Volumn 406, Issue 1-2, 2007, Pages 58-68

  Giordano, Daniela ^a   Vergara, Alessandro ^b   Caroline Lee, H ^c   Peisach, Jack ^c   Balestrieri, Marco ^a   Mazzarella, Lelio ^b   Parisi, Elio ^d   Prisco, Guido di ^a   Verde, Cinzia ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^d NONE

Author keywords

Antarctic; Arctic; Evolution; Hemoglobin; Structure; Unligated ferric state

Indexed keywords

AMINO ACID; GLOBIN; HEMOGLOBIN; ISOLEUCINE; PHOSPHATE; VALINE;

AMINO ACID SEQUENCE; ANTARCTICA; ARTICLE; BINDING SITE; BOHR EFFECT; CLADISTICS; ELECTRON SPIN RESONANCE; FISH; GENE FUNCTION; LIFESTYLE; MOLECULAR EVOLUTION; NONHUMAN; NUCLEOTIDE SEQUENCE; OXYGEN AFFINITY; PH MEASUREMENT; PHYLOGENY; PRIORITY JOURNAL; STRUCTURE ANALYSIS; SUBSTITUTION REACTION; TELEOST;

AMINO ACID SEQUENCE; ANIMALS; ARCTIC REGIONS; EVOLUTION, MOLECULAR; FISHES; GLOBINS; HEMOGLOBINS; MOLECULAR SEQUENCE DATA; OXYGEN; PHYLOGENY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

ANARHICHADIDAE; ANARHICHAS MINOR; COTTOIDEI; GADIDAE; LIPARIDAE (FISHES); LIPARIS TUNICATUS; NOTOTHENIOIDEI;

EID: 36749064392     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.06.002     Document Type: Article

References (42)

1. Abascal F., Zardoya R., and Posada D. ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21 (2005) 2104-2105
2. Blumberg W.E., and Peisach J. Low-spin ferric forms of hemoglobin and other heme proteins. Wenner-Gren Cent. Int. Symp. Ser. 18 (1972) 219-225
3. Bonaventura J., Gillen R.G., and Riggs A. The hemoglobin of the Crosspterygian fish, Latimeria chalumnae(Smith). Arch. Biochem. Biophys. 163 (1974) 728-734
4. Boffi A., Takahashi S., Spagnolo C., Rousseau D.L., and Chiancone E. Structural characterization of oxidized dimeric Scapharca inaequivalvis hemoglobin by resonance Raman spectroscopy. J. Biol. Chem. 269 (1994) 20437-20440
5. Brauer A.W., Oman C.L., and Margolies M.N. Use of o-phthalaldehyde to reduce background during automated Edman degradation. Anal. Biochem. 137 (1984) 134-142
6. Brey T., et al. Antarctic benthic diversity. Nature 368 (1994) 297
7. Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
8. Cupane A., et al. Modification of α-chain or β-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
9. Dayton P.K., Mordida B.J., and Bacon F. Polar marine communities. Am. Zool. 34 (1994) 90-99
10. D'Avino R., and di Prisco G. Antarctic fish haemoglobin: an outline of the molecular structure and oxygen binding properties. I. Molecular structure. Comp. Biochem. Physiol. 90B (1988) 579-584
11. D'Avino R., and di Prisco G. Haemoglobin from the Antarctic fish Notothenia coriiceps neglecta. 1. Purification and characterisation. Eur. J. Biochem. 179 (1989) 699-705
12. Dettaï A., and Lecointre G. In search for notothenioid (Teleostei) relatives. Antarct. Sci. 16 (2004) 71-85
13. 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
14. di Prisco G., Condò S.G., Tamburrini M., and Giardina B. Oxygen transport in extreme environments. Trends Biochem. Sci. 16 (1991) 471-474
15. Eastman J.T. Comparison of the Antarctic and Arctic fish faunas. Cybium 12 (1997) 276-287
16. Eastman J.T. The nature of the diversity of Antarctic fishes. Polar Biol. 28 (2005) 93-107
17. Eastman J.T., and McCune A.R. Fishes on the Antarctic continental shelf: evolution of a marine species flock?. J. Fish Biol. 57 Suppl. A (2000) 84-102
18. Guindon S., and Gascuel O. A simple, fast and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 52 (2003) 696-704
19. Ikeda-Saito M., et al. Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants. J. Biol. Chem. 267 (1992) 22843-22852
20. Ilari A., Bonamore A., Farina A., Johnson K., and Boffi A. The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket. J. Biol. Chem. 26 (2002) 23725-23732
21. Landon M. Cleavage at aspartyl-prolyl bonds. Methods Enzymol. 47 (1977) 145-149
22. Marmo Moreira L., Lima Poli A., Costa-Filho A.J., and Imasato H. Pentacoordinate and hexacoordinate ferric hemes in acid medium: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus. Biophys. Chem. 124 (2006) 62-72
23. 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
24. Mazzarella L., et al. Minimal structural requirements for Root effect: crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi. Proteins Struct. Funct. Bioinf. 62 (2006) 316-321
25. Miya M., et al. Major patterns of higher teleostean phylogenies: a new perspective based on 100 complete mitochondrial DNA sequences. Mol. Phylogenet. Evol. 26 (2003) 121-138
26. Nagai K., et al. Distal residues in the oxygen binding site of haemoglobin studied by protein engineering. Nature 329 (1987) 858-860
27. Quillin M., Arduini R., Olson J., and Phillips G.J. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J. Mol. Biol. 234 (1993) 140-155
28. Rambaut A., and Grassly N.C. Seq-gen: an application for the Monte Carlo simulation of DNA sequence evolution along phylogenetic tree. Comput. Appl. Biosci. 13 (1997) 235-238
29. Rodewald K., Stangl A., and Braunitzer G. Primary structure, biochemical and physiological aspects of hemoglobin from South American lungfish (Lepidosiren paradoxus, Dipnoi). Hoppe Seylers Z. Physiol. Chem. 365 (1984) 639-649
30. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: a Laboratory Manual. 2nd edn. (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
31. Smulevich G., Feis A., and Howes B.D. Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned?. Acc. Chem. Res. 38 (2005) 433-440
32. 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
33. Tamburrini M., Brancaccio A., Ippoliti R., and di Prisco G. The amino acid sequence and oxygen-binding properties of the single haemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps. Arch. Biochem. Biophys. 292 (1992) 295-302
34. Tamburrini M., Condò S.G., di Prisco G., and Giardina B. Adaptation to estreme environments: structure-function relationships in Emperor penguin haemoglobin. J. Mol. Biol. 237 (1994) 615-621
35. Tamburrini M., D'Avino R., Fago A., Carratore V., Kunzmann A., and di Prisco G. The unique haemoglobin system of Pleuragramma antarcticum, an Antarctic migratory teleost: structure and function of the three components. J. Biol. Chem. 271 (1996) 23780-23785
36. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
37. 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
38. Verde C., Balestrieri M., de Pascale D., Pagnozzi D., Lecointre G., and di Prisco G. The oxygen-transport system in three species of the boreal fish family Gadidae. Molecular phylogeny of haemoglobin. J. Biol. Chem. 281 (2006) 22073-22084
39. Verde C., Parisi E., and di Prisco G. The evolution of hemoglobin of thermal adaptation in polar fish. Gene 385 (2006) 137-145
40. Vergara, A., Franzese, M., Merlino, A., Vitagliano, L., Verde, C., di Prisco, G., Lee, H.C., Peisach, J., Mazzarella, L., in press. Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder Notothenioidei. Biophys. J. doi:10.1529/biophysj.107.105700.
41. Weber R.E., Jensen F.B., and Cox R.P. Analysis of teleost haemoglobin by Adair and Monod-Wyman-Changeux models: effects of nucleoside triphosphates and pH on oxygenation of tench haemoglobin. J. Comp. Physiol., B 157 (1987) 145-152
42. Weber R.E., et al. Isohemoglobin differentiation in the bimodal-breathing Amazon catfish Hoplosternum littorale. J. Biol. Chem. 275 (2000) 17297-17305