메뉴 건너뛰기




Volumn 121, Issue 7-8, 2004, Pages 753-769

Evolution of globin genes of the medaka Oryzias latipes (Euteleostei; Beloniformes; Oryziinae)

Author keywords

Adult globin; Embryonic globin; Globin gene evolution; Medaka; Oryzias latipes; Phylogenetic tree; Pseudogene; Teleost

Indexed keywords

GLOBIN;

EID: 2942522515     PISSN: 09254773     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mod.2004.03.035     Document Type: Article
Times cited : (31)

References (62)
  • 1
    • 0004253604 scopus 로고    scopus 로고
    • (Molphy2.3beta3 for UNIX-OS, ftp://ftp.ism.ac.jp/pub/ISMLIB/MOLPHY/; Molphy2.3beta3 for PC-OS ; Molphy2.3beta3 for PC-OS)
    • Adachi, J., Hasegawa, M., 1996. MOLPHY version 2.3 (Molphy2.3beta3 for UNIX-OS, ftp://ftp.ism.ac.jp/pub/ISMLIB/MOLPHY/; Molphy2.3beta3 for PC-OS, http://dmg.nott.ac.uk/software/software.htm).
    • (1996) MOLPHY Version 2.3
    • Adachi, J.1    Hasegawa, M.2
  • 4
    • 0032555240 scopus 로고    scopus 로고
    • Antarctic fish hemoglobins: Evidence for adaptive evolution at subzero temperature
    • Bargelloni L., Marcato S., Patarnello T. Antarctic fish hemoglobins: evidence for adaptive evolution at subzero temperature. Proc. Natl Acad. Sci. USA. 95:1998;8670-8675
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8670-8675
    • Bargelloni, L.1    Marcato, S.2    Patarnello, T.3
  • 5
    • 0021101406 scopus 로고
    • Primary structure of hemoglobin from trout (Salmo irideus) amino acid sequence of the beta chain of trout Hb I
    • Barra D., Petruzzelli R., Bossa F., Brunori M. Primary structure of hemoglobin from trout (Salmo irideus) amino acid sequence of the beta chain of trout Hb I. Biochim. Biophys. Acta. 742:1983;72-77
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 72-77
    • Barra, D.1    Petruzzelli, R.2    Bossa, F.3    Brunori, M.4
  • 6
    • 0014985250 scopus 로고
    • Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood
    • Binotti I., Giovenco S., Giardina B., Antonini E., Brunori M., Wyman J. Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood. Arch. Biochem. Biophys. 142:1971;274-280
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 274-280
    • Binotti, I.1    Giovenco, S.2    Giardina, B.3    Antonini, E.4    Brunori, M.5    Wyman, J.6
  • 7
    • 0018174906 scopus 로고
    • Primary structure of hemoglobin from trout (Salmo irideus). Amino acid sequence of alpha chain of Hb trout I
    • Bossa F., Barra D., Petruzzelli R., Martini F., Brunori M. Primary structure of hemoglobin from trout (Salmo irideus). Amino acid sequence of alpha chain of Hb trout I. Biochim. Biophys. Acta. 536:1978;298-305
    • (1978) Biochim. Biophys. Acta , vol.536 , pp. 298-305
    • Bossa, F.1    Barra, D.2    Petruzzelli, R.3    Martini, F.4    Brunori, M.5
  • 8
    • 0032007132 scopus 로고    scopus 로고
    • Genetic variation and functional properties of Atlantic cod hemoglobins: Introducing a modified tonometric method for studying fragile hemoglobins
    • Brix O., Foras E., Strand I. Genetic variation and functional properties of Atlantic cod hemoglobins: introducing a modified tonometric method for studying fragile hemoglobins. Comp. Biochem. Physiol. A. Mol. Integr. Physiol. 119:1998;575-583
    • (1998) Comp. Biochem. Physiol. A. Mol. Integr. Physiol. , vol.119 , pp. 575-583
    • Brix, O.1    Foras, E.2    Strand, I.3
  • 10
    • 0028172520 scopus 로고
    • Phylogenetic relationships among eutherian orders estimated from inferred sequences of mitochondrial proteins: Instability of a tree based on a single gene
    • Cao Y., Adachi J., Janke A., Paabo S., Hasegawa M. Phylogenetic relationships among eutherian orders estimated from inferred sequences of mitochondrial proteins: instability of a tree based on a single gene. J. Mol. Evol. 39:1994;519-527
    • (1994) J. Mol. Evol. , vol.39 , pp. 519-527
    • Cao, Y.1    Adachi, J.2    Janke, A.3    Paabo, S.4    Hasegawa, M.5
  • 12
    • 0019170956 scopus 로고
    • Carp hemoglobin. II. The alkaline Bohr effect
    • Chien J.C.W., Mayo K.H. Carp hemoglobin. II. The alkaline Bohr effect. J. Biol. Chem. 255:1980;9800-9806
    • (1980) J. Biol. Chem. , vol.255 , pp. 9800-9806
    • Chien, J.C.W.1    Mayo, K.H.2
  • 16
    • 0026659611 scopus 로고
    • The hemoglobins of marine and freshwater fish: The search for correlations with physiological adaptation
    • di Prisco G., Tamburrini M. The hemoglobins of marine and freshwater fish: the search for correlations with physiological adaptation. Comp. Biochem. Physiol. B. 102:1992;661-671
    • (1992) Comp. Biochem. Physiol. B , vol.102 , pp. 661-671
    • Di Prisco, G.1    Tamburrini, M.2
  • 18
    • 0018287874 scopus 로고
    • Isolation of the chicken beta-globin gene and a linked embryonic beta-like globin gene from a chicken DNA recombinant library
    • Dodgson J.B., Strommer J., Engel J.D. Isolation of the chicken beta-globin gene and a linked embryonic beta-like globin gene from a chicken DNA recombinant library. Cell. 17:1979;879-887
    • (1979) Cell , vol.17 , pp. 879-887
    • Dodgson, J.B.1    Strommer, J.2    Engel, J.D.3
  • 19
    • 0029163616 scopus 로고
    • The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity
    • Fago A., Carratore V., di Prisco G., Feuerlein R.J., Sottrup-Jensen L., Weber R.E. The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity. J. Biol. Chem. 270:1995;18897-188902
    • (1995) J. Biol. Chem. , vol.270 , pp. 18897-188902
    • Fago, A.1    Carratore, V.2    Di Prisco, G.3    Feuerlein, R.J.4    Sottrup-Jensen, L.5    Weber, R.E.6
  • 20
    • 0025162591 scopus 로고
    • Mapping of structural and transcription-related matrix attachment sites in the alpha-globin gene domain of avian erythroblasts and erythrocytess
    • Farache G., Razin S.V., Rzeszowska-Wolny J., Moreau J., Targa F.R., Scherrer K. Mapping of structural and transcription-related matrix attachment sites in the alpha-globin gene domain of avian erythroblasts and erythrocytess. Mol. Cell Biol. 10:1990;5349-5358
    • (1990) Mol. Cell Biol. , vol.10 , pp. 5349-5358
    • Farache, G.1    Razin, S.V.2    Rzeszowska-Wolny, J.3    Moreau, J.4    Targa, F.R.5    Scherrer, K.6
  • 23
    • 0001033232 scopus 로고
    • Protein sequences in phyologeny
    • F.J. Ayala. Sunderland, Massachusetts: Sinauer Associates Inc
    • Goodman M. Protein sequences in phyologeny. Ayala F.J. Molecular Evolution. 1976;141-159 Sinauer Associates Inc, Sunderland, Massachusetts
    • (1976) Molecular Evolution , pp. 141-159
    • Goodman, M.1
  • 24
    • 0016436505 scopus 로고
    • Darwinian evolution in the genealogy of haemoglobin
    • Goodman M., Moore G.W., Matsuda G. Darwinian evolution in the genealogy of haemoglobin. Nature. 253:1975;603-608
    • (1975) Nature , vol.253 , pp. 603-608
    • Goodman, M.1    Moore, G.W.2    Matsuda, G.3
  • 25
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
    • Hardison R. Hemoglobins from bacteria to man: evolution of different patterns of gene expression. J. Exp. Biol. 201:1998;1099-1117
    • (1998) J. Exp. Biol. , vol.201 , pp. 1099-1117
    • Hardison, R.1
  • 26
  • 27
    • 0020680868 scopus 로고
    • The Xenopus laevis globin gene family: Chromosomal arrangement and gene structure
    • Hosbach H.A., Wyler T., Weber R. The Xenopus laevis globin gene family: chromosomal arrangement and gene structure. Cell. 32:1983;45-53
    • (1983) Cell , vol.32 , pp. 45-53
    • Hosbach, H.A.1    Wyler, T.2    Weber, R.3
  • 28
    • 0028981025 scopus 로고
    • 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
    • Ito N., Komiyama N.H., 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
    • (1995) J Mol. Biol. , vol.250 , pp. 648-658
    • Ito, N.1    Komiyama, N.H.2    Fermi, G.3
  • 29
    • 0015924859 scopus 로고
    • Chemical and physiological properties of the larval and the larval hemoglobins in rainbow trout Salmo gairdnerii irideus
    • Iuchi I. Chemical and physiological properties of the larval and the larval hemoglobins in rainbow trout Salmo gairdnerii irideus. Comp. Biochem. Physiol. 44B:1973;1087-1101
    • (1973) Comp. Biochem. Physiol. , vol.44 , pp. 1087-1101
    • Iuchi, I.1
  • 30
    • 0001859865 scopus 로고
    • Cellular and molecular bases of the larval-adult shift of hemoglobins in fish
    • Iuchi I. Cellular and molecular bases of the larval-adult shift of hemoglobins in fish. Zool. Sci. 2:1985;11-23
    • (1985) Zool. Sci. , vol.2 , pp. 11-23
    • Iuchi, I.1
  • 31
    • 0000114779 scopus 로고
    • Electrophoretic pattern of larval hemoglobins of the salmonid fish Salmo aigrnerii irideus
    • Iuchi I., Yamagami K. Electrophoretic pattern of larval hemoglobins of the salmonid fish Salmo aigrnerii irideus. Comp. Biochem. Physiol. 28:1969;977-979
    • (1969) Comp. Biochem. Physiol. , vol.28 , pp. 977-979
    • Iuchi, I.1    Yamagami, K.2
  • 32
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D.T., Tayler W.R., Thornton J.M. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8:1992;275-282
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Tayler, W.R.2    Thornton, J.M.3
  • 34
    • 0032584670 scopus 로고    scopus 로고
    • Normal and abnormal protein subunit interactions in hemoglobins
    • Manning J.M., Dumoulin A., Li X., Manning L.R. Normal and abnormal protein subunit interactions in hemoglobins. J. Biol. Chem. 273:1998;9-19362
    • (1998) J. Biol. Chem. , vol.273 , pp. 9-19362
    • Manning, J.M.1    Dumoulin, A.2    Li, X.3    Manning, L.R.4
  • 35
    • 0032744810 scopus 로고    scopus 로고
    • Characterization and expression of embryonic globin in the rainbow trout. Oncorhynchus mykiss: Intra-embryonic initiation of erythropoiesis
    • Maruyama K., Yasumasu S., Iuchi I. Characterization and expression of embryonic globin in the rainbow trout. Oncorhynchus mykiss: intra-embryonic initiation of erythropoiesis. Dev. Growth Differ. 41:1999;589-599
    • (1999) Dev. Growth Differ. , vol.41 , pp. 589-599
    • Maruyama, K.1    Yasumasu, S.2    Iuchi, I.3
  • 36
    • 0036773779 scopus 로고    scopus 로고
    • Characterization and expression of embryonic or adult globins of the teleost (medaka Oryzias latipes)
    • Maruyama K., Yasumasu S., Iuchi I. Characterization and expression of embryonic or adult globins of the teleost (medaka Oryzias latipes). J. Biochem. 132:2002;581-589
    • (2002) J. Biochem. , vol.132 , pp. 581-589
    • Maruyama, K.1    Yasumasu, S.2    Iuchi, I.3
  • 37
    • 2942550796 scopus 로고    scopus 로고
    • Genomic organization and developmental expression of globin genes in the teleost Oryzias latipes
    • (in press)
    • Maruyama K., Yasumasu S., Naruse K., Mitani H., Shima A., Iuchi I. Genomic organization and developmental expression of globin genes in the teleost Oryzias latipes. Gene. 2004:2004;. (in press)
    • (2004) Gene , vol.2004
    • Maruyama, K.1    Yasumasu, S.2    Naruse, K.3    Mitani, H.4    Shima, A.5    Iuchi, I.6
  • 39
    • 0030828814 scopus 로고    scopus 로고
    • Head-to-head linkage of carp alpha- and beta-globin genes
    • Miyata M., Aoki T. Head-to-head linkage of carp alpha- and beta-globin genes. Biochim. Biophys. Acta. 1354:1997;127-133
    • (1997) Biochim. Biophys. Acta , vol.1354 , pp. 127-133
    • Miyata, M.1    Aoki, T.2
  • 40
    • 0029883426 scopus 로고    scopus 로고
    • Structural organization and sequence analysis of the globin locus in Atlantic salmon
    • McMorrow T., Wagner A., Deryckere F., Gannon F. Structural organization and sequence analysis of the globin locus in Atlantic salmon. DNA Cell Biol. 15:1996;407-414
    • (1996) DNA Cell Biol. , vol.15 , pp. 407-414
    • McMorrow, T.1    Wagner, A.2    Deryckere, F.3    Gannon, F.4
  • 43
    • 0018942757 scopus 로고
    • Internal organization of the major adult alpha- and beta-globin genes of X. laevis
    • Patient R.K., Elkington J.A., Kay R.M., Williams J.G. Internal organization of the major adult alpha- and beta-globin genes of X. laevis. Cell. 21:1980;565-573
    • (1980) Cell , vol.21 , pp. 565-573
    • Patient, R.K.1    Elkington, J.A.2    Kay, R.M.3    Williams, J.G.4
  • 46
    • 0024672322 scopus 로고
    • Amino acid sequence of alpha-chain of hemoglobin IV from trout (Salmo irideus)
    • Petruzzelli R., Barra D., Sensi L., Bossa F., Brunori M. Amino acid sequence of alpha-chain of hemoglobin IV from trout (Salmo irideus). Biochim. Biophys. Acta. 995:1989;255-258
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 255-258
    • Petruzzelli, R.1    Barra, D.2    Sensi, L.3    Bossa, F.4    Brunori, M.5
  • 47
    • 0032581710 scopus 로고    scopus 로고
    • A retrotransposon family from the pufferfish (fugu) Fugu rubripes
    • Poulter R., Butler M. A retrotransposon family from the pufferfish (fugu) Fugu rubripes. Gene. 215:1998;241-249
    • (1998) Gene , vol.215 , pp. 241-249
    • Poulter, R.1    Butler, M.2
  • 48
    • 0020363734 scopus 로고
    • The structure of the human zeta-globin gene and a closely linked, nearly identical pseudogene
    • Proudfoot N.J., Gil A., Maniatis T. The structure of the human zeta-globin gene and a closely linked, nearly identical pseudogene. Cell. 31:1982;553-563
    • (1982) Cell , vol.31 , pp. 553-563
    • Proudfoot, N.J.1    Gil, A.2    Maniatis, T.3
  • 49
    • 0033065523 scopus 로고    scopus 로고
    • A new beta-globin gene from the zebrafish, betaE1, and its pattern of transcription during embryogenesis
    • Quinkertz A., Campos-Ortega J.A. A new beta-globin gene from the zebrafish, betaE1, and its pattern of transcription during embryogenesis. Dev. Genes. Evol. 209:1999;126-131
    • (1999) Dev. Genes. Evol. , vol.209 , pp. 126-131
    • Quinkertz, A.1    Campos-Ortega, J.A.2
  • 50
    • 77956861509 scopus 로고
    • Properties of fish hemoglobins
    • W.S. Hoar, Randall D.J. New Yolk: Academic Press
    • Riggs A.A. Properties of fish hemoglobins. Hoar W.S., Randall D.J. Fish Physiology. Vol. 4:1970;209-252 Academic Press, New Yolk
    • (1970) Fish Physiology , vol.4 , pp. 209-252
    • Riggs, A.A.1
  • 51
    • 0032052760 scopus 로고    scopus 로고
    • Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins
    • Riggs A.F. Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins. J. Exp. Biol. 201:1998;1073-1084
    • (1998) J. Exp. Biol. , vol.201 , pp. 1073-1084
    • Riggs, A.F.1
  • 52
    • 0001063415 scopus 로고
    • Vertebrates without erythrocytes and blood pigment
    • Ruud J.T. Vertebrates without erythrocytes and blood pigment. Nature. 173:1954;848-850
    • (1954) Nature , vol.173 , pp. 848-850
    • Ruud, J.T.1
  • 53
    • 0027280835 scopus 로고
    • A mutagenic study of the allosteric linkage of His(HC3)146 beta in haemoglobin
    • Shih D.T., Luisi B.F., Miyazaki G., Perutz M.F., Nagai K. A mutagenic study of the allosteric linkage of His(HC3)146 beta in haemoglobin. J. Mol. Biol. 230:1993;1291-1296
    • (1993) J. Mol. Biol. , vol.230 , pp. 1291-1296
    • Shih, D.T.1    Luisi, B.F.2    Miyazaki, G.3    Perutz, M.F.4    Nagai, K.5
  • 55
    • 0030596491 scopus 로고    scopus 로고
    • The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms
    • Tame J.R., Wilson J.C., Weber R.E. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. J. Mol. Biol. 259:1996;749-760
    • (1996) J. Mol. Biol. , vol.259 , pp. 749-760
    • Tame, J.R.1    Wilson, J.C.2    Weber, R.E.3
  • 56
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 57
    • 0035539620 scopus 로고    scopus 로고
    • Erythropoiesis and conversion of RBCs and hemoglobins from larval and adult type during amphibian development
    • Wakahara M., Yamaguchi M. Erythropoiesis and conversion of RBCs and hemoglobins from larval and adult type during amphibian development. Zool. Sci. 18:2001;891-904
    • (2001) Zool. Sci. , vol.18 , pp. 891-904
    • Wakahara, M.1    Yamaguchi, M.2
  • 58
    • 0017230736 scopus 로고
    • Physiological properties of eel haemoglobin: Hypoxic acclimation, phosphate effects and multiplicity
    • Weber R.E., Lykkeboe G., Johansen K. Physiological properties of eel haemoglobin: hypoxic acclimation, phosphate effects and multiplicity. J. Exp. Biol. 64:1976;75-88
    • (1976) J. Exp. Biol. , vol.64 , pp. 75-88
    • Weber, R.E.1    Lykkeboe, G.2    Johansen, K.3
  • 61
    • 0031132687 scopus 로고    scopus 로고
    • Rapid communication: Nucleotide sequence of rainbow trout alpha-globin I and IV cDNA
    • Yoshizaki G., Takano A., Aoki T., Takashima F. Rapid communication: nucleotide sequence of rainbow trout alpha-globin I and IV cDNA. J. Anim. Sci. 75:1997;1426
    • (1997) J. Anim. Sci. , vol.75 , pp. 1426
    • Yoshizaki, G.1    Takano, A.2    Aoki, T.3    Takashima, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.