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Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships

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Abstract
Using a new template based on an alignment of 145 nonvertebrate globins we examined several recently determined sequences of putative globins and globin-like hemeproteins. We propose that all globins have evolved from a family of ancestral, approx. 17-kDa hemeproteins, which displayed the globin fold and functioned as redox proteins. Once atmospheric O-2 became available the acquisition of oxygen-binding properties was initiated, culminating in the various highly specialized functions known at present. During this evolutionary process, we suggest that (1) high oxygen affinity may have been acquired repeatedly and (2) the formation of chimeric proteins containing both a globin and a flavin binding domain was an additional and distinct evolutionary trend. Furthermore, globin-like hemeproteins encompass hemeproteins produced through convergent evolution from nonglobin ancestral proteins to carry out O-2-binding functions as well as hemeproteins whose sequences exhibit the loss of some or all of the structural determinants of the globin fold. We also propose that there occurred two cases of horizontal globin gene transfer, one from an ancestor common to the ciliates Paramecium and Tetrahymena and the green alga Chlamydomonas to a cyanobacterium ancestor and the other, from a eukaryote ancestor of the yeasts Saccharomyces and Candida to a bacterial ancestor of the proteobacterial genera Escherichia, Alcaligenes, and Vitreoscilla.
Keywords
structure, globins, evolution, horizontal gene transfer, HEMOGLOBIN-LIKE PROTEIN, AMINO-ACID-SEQUENCES, ESCHERICHIA-COLI, LIGAND-BINDING, DICROCOELIUM-DENDRITICUM, BACTERIAL HEMOGLOBIN, MOLECULAR-PROPERTIES, PARAMECIUM-CAUDATUM, REDUCTASE, KINETICS

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Chicago
Moens, Luc, Jacques Vanfleteren, Yves Van de Peer, Kris Peeters, Oscar Kapp, John Czeluzniak, Morris Goodman, Mark Blaxter, and Serge Vinogradov. 1996. “Globins in Nonvertebrate Species: Dispersal by Horizontal Gene Transfer and Evolution of the Structure-function Relationships.” Molecular Biology and Evolution 13 (2): 324–333.
APA
Moens, L., Vanfleteren, J., Van de Peer, Y., Peeters, K., Kapp, O., Czeluzniak, J., Goodman, M., et al. (1996). Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships. MOLECULAR BIOLOGY AND EVOLUTION, 13(2), 324–333.
Vancouver
1.
Moens L, Vanfleteren J, Van de Peer Y, Peeters K, Kapp O, Czeluzniak J, et al. Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships. MOLECULAR BIOLOGY AND EVOLUTION. 1996;13(2):324–33.
MLA
Moens, Luc, Jacques Vanfleteren, Yves Van de Peer, et al. “Globins in Nonvertebrate Species: Dispersal by Horizontal Gene Transfer and Evolution of the Structure-function Relationships.” MOLECULAR BIOLOGY AND EVOLUTION 13.2 (1996): 324–333. Print.
@article{186898,
  abstract     = {Using a new template based on an alignment of 145 nonvertebrate globins we examined several recently determined sequences of putative globins and globin-like hemeproteins. We propose that all globins have evolved from a family of ancestral, approx. 17-kDa hemeproteins, which displayed the globin fold and functioned as redox proteins. Once atmospheric O-2 became available the acquisition of oxygen-binding properties was initiated, culminating in the various highly specialized functions known at present. During this evolutionary process, we suggest that (1) high oxygen affinity may have been acquired repeatedly and (2) the formation of chimeric proteins containing both a globin and a flavin binding domain was an additional and distinct evolutionary trend. Furthermore, globin-like hemeproteins encompass hemeproteins produced through convergent evolution from nonglobin ancestral proteins to carry out O-2-binding functions as well as hemeproteins whose sequences exhibit the loss of some or all of the structural determinants of the globin fold. We also propose that there occurred two cases of horizontal globin gene transfer, one from an ancestor common to the ciliates Paramecium and Tetrahymena and the green alga Chlamydomonas to a cyanobacterium ancestor and the other, from a eukaryote ancestor of the yeasts Saccharomyces and Candida to a bacterial ancestor of the proteobacterial genera Escherichia, Alcaligenes, and Vitreoscilla.},
  author       = {Moens, Luc and Vanfleteren, Jacques and Van de Peer, Yves and Peeters, Kris and Kapp, Oscar and Czeluzniak, John and Goodman, Morris and Blaxter, Mark and Vinogradov, Serge},
  issn         = {0737-4038},
  journal      = {MOLECULAR BIOLOGY AND EVOLUTION},
  keyword      = {structure,globins,evolution,horizontal gene transfer,HEMOGLOBIN-LIKE PROTEIN,AMINO-ACID-SEQUENCES,ESCHERICHIA-COLI,LIGAND-BINDING,DICROCOELIUM-DENDRITICUM,BACTERIAL HEMOGLOBIN,MOLECULAR-PROPERTIES,PARAMECIUM-CAUDATUM,REDUCTASE,KINETICS},
  language     = {eng},
  number       = {2},
  pages        = {324--333},
  title        = {Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships},
  url          = {http://dx.doi.org/10.1093/oxfordjournals.molbev.a025592},
  volume       = {13},
  year         = {1996},
}

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