Conservation of the myoglobin gene among antarctic notothenioid fishes

Molecular Marine Biology and Biotechnology

Volumn 6, Issue 3, 1997, Pages 207-216

  Vayda, Michael E ^a   Small, Deena J ^a   Yuan, Meng Lan ^a,b   Costello, Lori ^a   Sidell, Bruce D ^a  

^a UNIVERSITY OF MAINE   (United States)

^b BOSTON CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; MYOGLOBIN;

AMINO ACID SEQUENCE; ANIMAL; ANTARCTICA; ARTICLE; CHEMISTRY; DNA SEQUENCE; FISH; GENE; GENETIC VARIABILITY; GENETICS; HEART MUSCLE; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYLOGENY; SEA;

AMINO ACID SEQUENCE; ANIMALS; ANTARCTIC REGIONS; BASE SEQUENCE; CONSERVED SEQUENCE; DNA, COMPLEMENTARY; FISHES; GENES; MOLECULAR SEQUENCE DATA; MYOCARDIUM; MYOGLOBIN; OCEANS AND SEAS; PHYLOGENY; RNA, MESSENGER; SEQUENCE ANALYSIS, DNA; VARIATION (GENETICS);

ANIMALIA; CHAENOCEPHALUS ACERATUS; CHAMPSOCEPHALUS GUNNARI; CHANNICHTHYIDAE; NOTOTHENIIDAE; PAGETOPSIS MACROPTERUS; PISCES; SALANGINI;

EID: 0031239677     PISSN: 10536426     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (48)

1. Acierno, R., Agnisola, C., Tota, B., and Sidell, B.D. (1997). Myoglobin enhances cardiac performance in Antarctic icefish species that express the pigment. Am J Physiol 273(42):R100-R106.
2. Akaboshi, E. (1985a). Cloning of the human myoglobin gene. Gene 33:241-249.
3. Akaboshi, E. (1985b). Cloning and sequence analysis of porcine myoglobin cDNA. Gene 40:137-140.
4. Anderson, M.E. (1990). The origin and evolution of antarctic ichthyofauna. In: Gon, O., and Heemstra, P.C. (eds.). Fishes of the Southern Ocean, Grahamstown, S. Africa: JLB Smith Institute of Ichthyology, 26-33.
5. Bargelloni, L., Ritchie, P.A., Pararnello, T., Battaglia, B., Lambert, D.M., and Meyer, A. (1994). Molecular evolution at subzero temperatures: mitochondrial and nuclear phylogenies of fishes from Antarctica (suborder Notothenioidei) and the evolution of antifreeze. Mol Biol Evol 6:854-863.
6. Blanchetot, A., Wilson, V., Wood, D., and Jeffreys, A.J. (1983). The seal myoglobin gene: an unusually long globin gene. Nature 301:732-734.
7. Blanchetot, A., Price, M., and Jeffreys, A.J. (1986). The mouse globin myogene. Eur J Biochem 159:469-474.
8. Cashon, R.E., Vayda, M.E., and Sidell, B.D. (1997). Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures. Comp Biochem Physiol 117B:(in press).
9. Clarke, A. (1990). Temperature evolution: southern ocean cooling and the Antarctic marine fauna. In: Kerry, K.R., and Hempel, G. (eds.) Antarctic Ecosystems: Ecological Change and Conservation. Berlin, Germany: Springer, 9-22.
10. Cocca, E., Ratnayake-Lecamwasam, M., Parker, S.A., Camardella, L., Ciaramella, M., diPrisco, G., and Detrich, H.W. (1995). Genomic remnants of α-globin genes in the hemoglobinless antarctic icefishes. Proc Natl Acad Sci USA 92:1817-1821.
11. Dowd, M.K., Murali, R., and Seagrave, R.V. (1991). Effect of temperature on the myoglobin-facilitated transport of oxygen in skeletal muscle. Biophys J 60:160-171.
12. Driedzic, W.R., Stewart, M.J., and Scott, D.L. (1982). The protective effect of myoglobin during hypoxic perfusion of isolated fish hearts. J Mol Cell Cardiol 14:673-677.
13. Eastman, J.T. (1991). Evolution and diversification of Antarctic notothenioid fishes. Am Zool 31:93-109.
14. Eastman, J.T. (1993). Antarctic Fish Biology: Evolution in a Unique Environment. San Diego, Calif.: Academic Press.
15. Ekau, W. (1990). Demersal fish fauna of the Weddell Sea, Antarctica. Antarctic Sci 2:129-137.
16. Feller, G., and Gerday, C. (1987). Metabolic pattern of the heart of haemoglobin- and myoglobin-free Antarctic fish, Channichthys rhinoceratus. Polar Biol 7:225-229.
17. Feller, G., Poncin, A., Aittaleb, M., Schyns, R., and Gerday, C. (1994). The blood proteins of the Antarctic icefish Channichthys rhinoceratus: biological significance and purification of the two main components. Comp Biochem Physiol 109B:89-97.
18. Hamoir, G. (1988). Biochemical adaptation of the muscles of the Channichthyidae to their lack in hemoglobin and myoglobin. Comp Biochem Physiol 90B:557-559.
19. Hamoir, G., and Gerardin-Otthiers, N. (1980). Differentiation of the sarcoplasmic proteins of white, yellowish and cardiac muscles of an Antarctic hemoglobin-free fish, Champsocephalus gunnari. Comp Biochem Physiol 65B:199-206.
20. Hemmingsen, E.A. (1991). Respiratory and cardiovascular adaptation in hemoglobin-free fish: resolved and unresolved problems. In: di Prisco, G., Maresca, B., and Tota, B. (eds.). Biology of Antarctic Fish. New York, N.Y.: Springer-Verlag, p 191-203.
21. Higgins, D.G. (1994). CLUSTAL V: multiple alignment of DNA and protein sequences. Methods Mol Biol 25:307-318.
22. Higgins, D.G., and Sharp, P.M. (1988). CLUSTAL: a package for performing multiple sequence alignment on a micro-computer. Gene 73:237-244.
23. Iwami, T. (1985). Osteology and relationships of the family Channichthyidae. Mem Natl Inst Polar Res, Tokyo Ser E 36:1-69.
24. Johnston, I.A., Fitch, N., Zummo, G., Wood, R.E., Harrison, P., and Tota, B. (1983). Morphometric and ultrastructural features of the ventricular myocardium of the haemoglobin-less icefish Chaenocephalus aceratus. Comp Biochem Physiol 76A:475-480.
25. Kennett, J.P. (1977). Cenozoic evolution of Antarctic glaciation, the circum-Antarctic Ocean, and their impact of global paleocenography. J Geophys Res 82:3843-3860.
26. Kennett, J.P. (1982). Marine Geology. Englewood Cliffs, N.J.: Prentice-Hall.
27. Kimura, M. (1980). A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences. Mol Evol 16:111-120.
28. Kozak, M. (1986). Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Proc Natl Acad Sci USA 83: 2850-2853.
29. Kumar, S., Tamura, K., and Nei, M. (1993). MEGA: Molecular evolutionary genetics analysis, version 1.0. University Park: The Pennsylvania State University.
30. Li, W.-H., Wu, C.-I., and Luo, C.-C. (1985). A new method for estimating synonymous and nonsynonymous rates of nucleotide substitution considering the relative likelihood of nucleotide and codon changes. Mol Biol Evol 3:150-174.
31. Lim, S.-K., and Maquat, L.E. (1992). Human β-globin mRNAs that harbor a nonsense codon are degraded in murine erythroid tissues to intermediates lacking regions of exon I or exons I or II that have a cap-like structure at the 5′ termini. EMBO J 11:3271-3278.
32. Lim, S.-K., Sigmund, C.D., Gross, K.W., and Maquat, L.W. (1992). Nonsense codons in human β-globin mRNA result in the production of mRNA degradation products. Mol Cell Biol 12:1149-1161.
33. Londraville, R.L., and Sidell, B.D. (1990). Maximal diffusion-distance within skeletal muscle can be estimated from mitochondrial distributions. Respir Physiol 81:291-302.
34. Nichols, J.W., and Weber, L.J. (1989a). Oxidation of cardiac myoglobin in vivo by sodium nitrite or hydroxylamine. Arch Toxicol 6:484-488.
35. Nichols, J.W., and Weber, L.J. (1989b). Comparative oxygen affinity of fish and mammalian myoglobins. J Comp Physiol B 159:205-209.
36. Ruud, J.T. (1954). Vertebrates without erythrocytes and blood pigment. Nature 173:848-850.
37. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning. A Laboratory Manual, 2nd ed. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory.
38. Sato, F., Shiro, Y., Sachaguchi, Y., Lizuka, T., and Hayashi, H. (1990). Thermodynamic study of protein dynamic structure in the oxygen binding reaction of myoglobin. J Biol Chem 265:18823-18828.
39. Sheets, M.D., Ogg, S.C., and Wickens, M.P. (1990). Point mutations in AAUAAA and the poly(A) addition site: effects on the accuracy and efficiency of cleavage and polyadenylation in vitro. Nucleic Acids Res 18:5799-5805.
40. Shirras, A., and Northcote, D. (1984). Molecular cloning and characterization of DNA complementary to mRNA from wounded Solanum tuberosum tuber tissue. Planta 162: 353-360.
41. Sidell, B.D., Vayda, M.E., Small, D.J., Moylan, T.J., Londraville, R.L., Yuan, M.-L., Rodnick, K.J., Eppley, Z.A., and Costello, L. (1997). Variable expression of myoglobin among the hemoglobinless Antarctic icefishes. Proc Natl Acad Sci USA 94:3420-3424.
42. Stevens, E.D., and Carey, F.G. (1981). One why of the warmth of warm-bodied fish. Am J Physiol 240:R151-R155.
43. Swofford, D.L. (1993). PAUP: Phylogenetic analysis using parsimony, version 3.1. Computer program distributed by the Illinois Natural History Survey, Champaign, Ill.
44. Trout, A.B. (1994). Ligation-anchored PCR. In: Griffin, H.G., and Griffin, A.M. (eds.). PCR Technology, Current Innovations. Boca Raton, Fla.: CRC Press, 141-146.
45. Vayda, M.E., Small, D.J., and Sidell, B.D. (1997). Expression of the myoglobin gene in Antarctic channichthyid fishes. In: Battaglia, B., Valencia, J., and Walton, D.W.H. (eds.). VI SCAR Antarctic Communities. Cambridge, U.K.: Cambridge University Press, pp. 57-62.
46. Watts, D.A., Rice, R.H., and Brown, W.D. (1980). The primary structure of myoglobin from yellowfin tuna Thunnus albacares. J Biol Chem 255:10916-10924.
47. Weller, P., Jeffreys, A.J., Wilson, V., and Blanchetot, A. (1984). Organization of the human myoglobin gene. EMBO J 3:439-446.
48. Wittenberg, J.B. (1970). Myoglobin facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. Physiol Rev 50:559-636.