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Volumn 5, Issue 7, 2013, Pages 1435-1442

A broad genomic survey reveals multiple origins and frequent losses in the evolution of respiratory hemerythrins and hemocyanins

Author keywords

Comparative genomics; Hemerythrin; Hemocyanin; Lateral gene transfer; Respiration; Tyrosinase

Indexed keywords

HEMERYTHRIN; HEMOCYANIN; MONOPHENOL MONOOXYGENASE; TRANSCRIPTOME;

EID: 84891681622     PISSN: None     EISSN: 17596653     Source Type: Journal    
DOI: 10.1093/gbe/evt102     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 79955910093 scopus 로고    scopus 로고
    • Evolution and metabolic significance of the urea cycle in photosynthetic diatoms
    • Allen AE, et al. 2011. Evolution and metabolic significance of the urea cycle in photosynthetic diatoms. Nature 473:203-207.
    • (2011) Nature , vol.473 , pp. 203-207
    • Allen, A.E.1
  • 2
    • 84866912587 scopus 로고    scopus 로고
    • A "neural" enzyme in nonbilaterian animals and algae: Preneural origins for peptidylglycine alpha-amidating monooxygenase
    • Attenborough RM, Hayward DC, Kitahara MV, Miller DJ, Ball EE. 2012. A "neural" enzyme in nonbilaterian animals and algae: preneural origins for peptidylglycine alpha-amidating monooxygenase. Mol Biol Evol. 29:3095-3109.
    • (2012) Mol Biol Evol. , vol.29 , pp. 3095-3109
    • Attenborough, R.M.1    Hayward, D.C.2    Kitahara, M.V.3    Miller, D.J.4    Ball, E.E.5
  • 3
    • 0026616956 scopus 로고
    • Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech
    • Baert JL, Britel M, Sautiere P, Malecha J. 1992. Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech. Eur J Biochem. 209:563-569.
    • (1992) Eur J Biochem. , vol.209 , pp. 563-569
    • Baert, J.L.1    Britel, M.2    Sautiere, P.3    Malecha, J.4
  • 4
    • 52949107602 scopus 로고    scopus 로고
    • A phylogenomic profile of hemerythrins, the nonheme diiron binding respiratory proteins
    • Bailly X, Vanin S, Chabasse C, Mizuguchi K, Vinogradov SN. 2008. A phylogenomic profile of hemerythrins, the nonheme diiron binding respiratory proteins. BMC Evol Biol. 8:244.
    • (2008) BMC Evol Biol. , vol.8 , pp. 244
    • Bailly, X.1    Vanin, S.2    Chabasse, C.3    Mizuguchi, K.4    Vinogradov, S.N.5
  • 5
    • 84867830765 scopus 로고    scopus 로고
    • Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor
    • Blank M, Burmester T. 2012. Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor. Mol Biol Evol. 29:3553-3561.
    • (2012) Mol Biol Evol. , vol.29 , pp. 3553-3561
    • Blank, M.1    Burmester, T.2
  • 6
    • 77957212137 scopus 로고
    • Hemocyanins - Relationships in their structure, function and assembly
    • Bonaventura J, Bonaventura C. 1980. Hemocyanins - relationships in their structure, function and assembly. Am Zool. 20:7-17.
    • (1980) Am Zool. , vol.20 , pp. 7-17
    • Bonaventura, J.1    Bonaventura, C.2
  • 7
    • 0035140529 scopus 로고    scopus 로고
    • Molecular evolution of the arthropod hemocyanin super family
    • Burmester T. 2001. Molecular evolution of the arthropod hemocyanin super family. Mol Biol Evol. 18:184-195.
    • (2001) Mol Biol Evol. , vol.18 , pp. 184-195
    • Burmester, T.1
  • 8
    • 80155198843 scopus 로고    scopus 로고
    • The mysterious evolutionary origin for the GNE gene and the root of bilateria
    • de Mendoza A, Ruiz-Trillo I. 2011. The mysterious evolutionary origin for the GNE gene and the root of bilateria. Mol Biol Evol. 28:2987-2991.
    • (2011) Mol Biol Evol. , vol.28 , pp. 2987-2991
    • De Mendoza, A.1    Ruiz-Trillo, I.2
  • 9
    • 0027365751 scopus 로고
    • Amino acid sequence of the small cadmium-binding protein (MP II) from Nereis diversicolor (annelida, polychaeta). Evidence for a myohemerythrin structure
    • Demuynck S, Li KW, Van der Schors R, Dhainaut-Courtois N. 1993. Amino acid sequence of the small cadmium-binding protein (MP II) from Nereis diversicolor (annelida, polychaeta). Evidence for a myohemerythrin structure. Eur J Biochem. 217:151-156.
    • (1993) Eur J Biochem. , vol.217 , pp. 151-156
    • Demuynck, S.1    Li, K.W.2    Van Der Schors, R.3    Dhainaut-Courtois, N.4
  • 10
    • 84859952425 scopus 로고    scopus 로고
    • New insights into the evolution of metazoan tyrosinase gene family
    • Esposito R, et al. 2012. New insights into the evolution of metazoan tyrosinase gene family. PLoS One 7:e35731.
    • (2012) PLoS One , vol.7
    • Esposito, R.1
  • 11
    • 38349117475 scopus 로고    scopus 로고
    • Diversity and distribution of hemerythrin-like proteins in prokaryotes
    • French CE, Bell JM, Ward FB. 2008. Diversity and distribution of hemerythrin-like proteins in prokaryotes. FEMS Microbiol Lett. 279: 131-145.
    • (2008) FEMS Microbiol Lett. , vol.279 , pp. 131-145
    • French, C.E.1    Bell, J.M.2    Ward, F.B.3
  • 12
    • 4143101579 scopus 로고    scopus 로고
    • Hypoxia-induced synthesis of hemoglobin in the crustacean Daphnia magna is hypoxia-inducible factor-dependent
    • Gorr TA, Cahn JD, Yamagata H, Bunn HF. 2004. Hypoxia-induced synthesis of hemoglobin in the crustacean Daphnia magna is hypoxia-inducible factor-dependent. J Biol Chem. 279:36038-36047.
    • (2004) J Biol Chem. , vol.279 , pp. 36038-36047
    • Gorr, T.A.1    Cahn, J.D.2    Yamagata, H.3    Bunn, H.F.4
  • 13
    • 1642308130 scopus 로고    scopus 로고
    • Putative phenoloxidases in the tunicate Ciona intestinalis and the origin of the arthropod hemocyanin superfamily
    • Immesberger A, Burmester T. 2004. Putative phenoloxidases in the tunicate Ciona intestinalis and the origin of the arthropod hemocyanin superfamily. J Comp Physiol B. 174:169-180.
    • (2004) J Comp Physiol B. , vol.174 , pp. 169-180
    • Immesberger, A.1    Burmester, T.2
  • 15
    • 18944380045 scopus 로고    scopus 로고
    • Characterization of a prokaryotic hemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath)
    • Karlsen OA, et al. 2005. Characterization of a prokaryotic hemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath). FEBS J. 272:2428-2440.
    • (2005) FEBS J. , vol.272 , pp. 2428-2440
    • Karlsen, O.A.1
  • 16
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K, Misawa K, Kuma K, Miyata T. 2002. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 30:3059-3066.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 17
    • 0033537978 scopus 로고    scopus 로고
    • Heterogeneity and differential expression under hypoxia of two domain hemoglobin chains in the water flea, Daphnia magna
    • Kimura S, Tokishita S, Ohta T, Kobayashi M, Yamagata H. 1999. Heterogeneity and differential expression under hypoxia of two domain hemoglobin chains in the water flea, Daphnia magna. J Biol Chem. 274:10649-10653.
    • (1999) J Biol Chem. , vol.274 , pp. 10649-10653
    • Kimura, S.1    Tokishita, S.2    Ohta, T.3    Kobayashi, M.4    Yamagata, H.5
  • 18
    • 2442691520 scopus 로고    scopus 로고
    • A Bayesian mixture model for across-site heterogeneities in the amino-acid replacement process
    • Lartillot N, Philippe H. 2004. A Bayesian mixture model for across-site heterogeneities in the amino-acid replacement process. Mol Biol Evol. 21:1095-1109.
    • (2004) Mol Biol Evol. , vol.21 , pp. 1095-1109
    • Lartillot, N.1    Philippe, H.2
  • 19
    • 52049119243 scopus 로고    scopus 로고
    • Hemocyanin in mollusks - A molecular survey and new data on hemocyanin genes in Solenogastres and Caudofoveata
    • Lieb B, Todt C. 2008. Hemocyanin in mollusks - a molecular survey and new data on hemocyanin genes in Solenogastres and Caudofoveata. Mol Phylogenet Evol. 49:382-385.
    • (2008) Mol Phylogenet Evol. , vol.49 , pp. 382-385
    • Lieb, B.1    Todt, C.2
  • 20
    • 33747080785 scopus 로고    scopus 로고
    • Red blood with blue-blood ancestry: Intriguing structure of a snail hemoglobin
    • Lieb B, et al. 2006. Red blood with blue-blood ancestry: intriguing structure of a snail hemoglobin. Proc Natl Acad Sci U S A. 103:12011-12016.
    • (2006) Proc Natl Acad Sci U S A. , vol.103 , pp. 12011-12016
    • Lieb, B.1
  • 21
    • 71849094540 scopus 로고    scopus 로고
    • Respiratory proteins in Sipunculus nudus - Implications for phylogeny and evolution of the hemerythrin family
    • Meyer A, Lieb B. 2010. Respiratory proteins in Sipunculus nudus - implications for phylogeny and evolution of the hemerythrin family. Comp Biochem Physiol B Biochem Mol Biol. 155:171-177.
    • (2010) Comp Biochem Physiol B Biochem Mol Biol. , vol.155 , pp. 171-177
    • Meyer, A.1    Lieb, B.2
  • 22
    • 79955125001 scopus 로고    scopus 로고
    • Genomic insights into Wnt signaling in an early divergingmetazoan, the ctenophore Mnemiopsis leidyi
    • Pang K, et al. 2010. Genomic insights into Wnt signaling in an early divergingmetazoan, the ctenophore Mnemiopsis leidyi. Evodevo 1:10.
    • (2010) Evodevo , vol.1 , pp. 10
    • Pang, K.1
  • 23
    • 10344243985 scopus 로고    scopus 로고
    • A globin gene of ancient evolutionary origin in lower vertebrates: Evidence for two distinct globin families in animals
    • Roesner A, Fuchs C, Hankeln T, Burmester T. 2005. A globin gene of ancient evolutionary origin in lower vertebrates: evidence for two distinct globin families in animals. Mol Biol Evol. 22:12-20.
    • (2005) Mol Biol Evol. , vol.22 , pp. 12-20
    • Roesner, A.1    Fuchs, C.2    Hankeln, T.3    Burmester, T.4
  • 24
    • 70350576223 scopus 로고    scopus 로고
    • An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis
    • Salahudeen AA, et al. 2009. An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis. Science 326: 722-726.
    • (2009) Science , vol.326 , pp. 722-726
    • Salahudeen, A.A.1
  • 26
    • 79952143437 scopus 로고    scopus 로고
    • Unexpected repertoire of metazoan transcription factors in the unicellular holozoan Capsaspora owczarzaki
    • Sebé -Pedrós A, de Mendoza A, Lang BF, Degnan BM, Ruiz-Trillo I. 2011. Unexpected repertoire of metazoan transcription factors in the unicellular holozoan Capsaspora owczarzaki. Mol Biol Evol. 28:1241-1254.
    • (2011) Mol Biol Evol. , vol.28 , pp. 1241-1254
    • Sebé-Pedrós, A.1    De Mendoza, A.2    Lang, B.F.3    Degnan, B.M.4    Ruiz-Trillo, I.5
  • 28
    • 77955490196 scopus 로고    scopus 로고
    • The Amphimedon queenslandica genome and the evolution of animal complexity
    • Srivastava M, et al. 2010. The Amphimedon queenslandica genome and the evolution of animal complexity. Nature 466:720-726.
    • (2010) Nature , vol.466 , pp. 720-726
    • Srivastava, M.1
  • 29
    • 79959401340 scopus 로고    scopus 로고
    • Eukaryotic pyruvate formate lyase and its activating enzymewere acquired laterally from a Firmicute
    • Stairs CW, Roger AJ, Hampl V. 2011. Eukaryotic pyruvate formate lyase and its activating enzymewere acquired laterally from a Firmicute.Mol Biol Evol. 28:2087-2099.
    • (2011) Mol Biol Evol. , vol.28 , pp. 2087-2099
    • Stairs, C.W.1    Roger, A.J.2    Hampl, V.3
  • 30
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • Stamatakis A. 2006. RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22:2688-2690.
    • (2006) Bioinformatics , vol.22 , pp. 2688-2690
    • Stamatakis, A.1
  • 31
    • 0035999729 scopus 로고    scopus 로고
    • Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects
    • Sugumaran M. 2002. Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell Res. 15:2-9.
    • (2002) Pigment Cell Res. , vol.15 , pp. 2-9
    • Sugumaran, M.1
  • 32
    • 33746271072 scopus 로고    scopus 로고
    • Ontogeny of crustacean respiratory proteins
    • Terwilliger NB, Ryan M. 2001. Ontogeny of crustacean respiratory proteins. Am Zool. 41:1057-1067.
    • (2001) Am Zool. , vol.41 , pp. 1057-1067
    • Terwilliger, N.B.1    Ryan, M.2
  • 33
    • 0032053156 scopus 로고    scopus 로고
    • Functional adaptations of oxygen-transport proteins
    • Terwilliger NB. 1998. Functional adaptations of oxygen-transport proteins. J Exp Biol. 201:1085-1098.
    • (1998) J Exp Biol. , vol.201 , pp. 1085-1098
    • Terwilliger, N.B.1
  • 34
    • 84863393257 scopus 로고    scopus 로고
    • Structural and molecular characterization of iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5)
    • Thompson JW, et al. 2012. Structural and molecular characterization of iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5). J Biol Chem. 287:7357-7365.
    • (2012) J Biol Chem. , vol.287 , pp. 7357-7365
    • Thompson, J.W.1
  • 35
  • 36
    • 31844441323 scopus 로고    scopus 로고
    • Molecular evolution and phylogeny of sipunculan hemerythrins
    • Vanin S, et al. 2006. Molecular evolution and phylogeny of sipunculan hemerythrins. J Mol Evol. 62:32-41.
    • (2006) J Mol Evol. , vol.62 , pp. 32-41
    • Vanin, S.1
  • 37
    • 70350613915 scopus 로고    scopus 로고
    • Control of iron homeostasis by an iron-regulated ubiquitin ligase
    • Vashisht AA, et al. 2009. Control of iron homeostasis by an iron-regulated ubiquitin ligase. Science 326:718-721.
    • (2009) Science , vol.326 , pp. 718-721
    • Vashisht, A.A.1
  • 38
    • 6344241109 scopus 로고    scopus 로고
    • Up-regulation of neurohemerythrin expression in the central nervous system of the medicinal leech, Hirudo medicinalis, following septic injury
    • Vergote D, et al. 2004. Up-regulation of neurohemerythrin expression in the central nervous system of the medicinal leech, Hirudo medicinalis, following septic injury. J Biol Chem. 279:43828-43837.
    • (2004) J Biol Chem. , vol.279 , pp. 43828-43837
    • Vergote, D.1
  • 39
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber RE, Vinogradov SN. 2001. Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol Rev. 81:569-628.
    • (2001) Physiol Rev. , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 40
    • 0034595406 scopus 로고    scopus 로고
    • A hemerythrin-like domain in a bacterial chemotaxis protein
    • Xiong J, Kurtz DM Jr, Ai J, Sanders-Loehr J. 2000. A hemerythrin-like domain in a bacterial chemotaxis protein. Biochemistry 39: 5117-5125.
    • (2000) Biochemistry , vol.39 , pp. 5117-5125
    • Xiong, J.1    Kurtz Jr., D.M.2    Ai, J.3    Sanders-Loehr, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.