Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes

Autores
De Souza, F.S.J.; Bumaschny, V.F.; Low, M.J.; Rubinstein, M.
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The proopiomelanocortin gene (POMC) encodes several bioactive peptides, including adrenocorticotropin hormone, α-, β-, and γ-melanocyte-stimulating hormone, and the opioid peptide β-endorphin, which play key roles in vertebrate physiology. In the human, mouse, and chicken genomes, there is only one POMC gene. By searching public genome projects, we have found that Tetraodon (Tetraodon nigroviridis), Fugu (Takifugu rubripes), and zebrafish (Danio rerio) possess two POMC genes, which we called POMCα and POMCβ, and we present phylogenetic and mapping evidence that these paralogue genes originated in the whole-genome duplication specific to the teleost lineage over 300 MYA. In addition, we present evidence for two types of subfunction partitioning between the paralogues. First, in situ hybridization experiments indicate that the expression domains of the ancestral POMC gene have been subfunctionalized in Tetraodon, with POMCα expressed in the nucleus lateralis tuberis of the hypothalamus, as well as in the rostral pars distalis and pars intermedia (PI) of the pituitary, whereas POMCβ is expressed in the preoptic area of the brain and weakly in the pituitary PI. Second, POMCβ genes have a β-endorphin segment that lacks the consensus opioid signal and seems to be under neutral evolution in tetraodontids, whereas POMCα genes possess well-conserved peptide regions. Thus, POMC paralogues have experienced subfunctionalization of both expression and peptide domains during teleost evolution. The study of regulatory regions of fish POMC genes might shed light on the mechanisms of enhancer partitioning between duplicate genes, as well as the roles of POMC-derived peptides in fish physiology.
Fil:Rubinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Mol. Biol. Evol. 2005;22(12):2417-2427
Materia
β-endorphin
Evolution
POMC
Subfunctionalization
Teleosts
Tetraodon
opiate
proopiomelanocortin
article
gene duplication
gene mapping
hypophysis
hypothalamus nucleus
in situ hybridization
molecular evolution
nonhuman
nucleotide sequence
phylogeny
preoptic area
protein domain
protein expression
protein function
signal transduction
teleost
Amino Acid Sequence
Animals
Evolution, Molecular
Fishes
Gene Duplication
Molecular Sequence Data
Phylogeny
Pro-Opiomelanocortin
Sequence Alignment
Tetraodontiformes
Zebrafish
Danio rerio
Takifugu
Takifugu rubripes
Teleostei
Tetraodon
Tetraodon nigroviridis
Tetraodontidae
Vertebrata
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_07374038_v22_n12_p2417_DeSouza

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oai_identifier_str paperaa:paper_07374038_v22_n12_p2417_DeSouza
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishesDe Souza, F.S.J.Bumaschny, V.F.Low, M.J.Rubinstein, M.β-endorphinEvolutionPOMCSubfunctionalizationTeleostsTetraodonopiateproopiomelanocortinarticlegene duplicationgene mappinghypophysishypothalamus nucleusin situ hybridizationmolecular evolutionnonhumannucleotide sequencephylogenypreoptic areaprotein domainprotein expressionprotein functionsignal transductionteleostAmino Acid SequenceAnimalsEvolution, MolecularFishesGene DuplicationMolecular Sequence DataPhylogenyPro-OpiomelanocortinSequence AlignmentTetraodontiformesZebrafishDanio rerioTakifuguTakifugu rubripesTeleosteiTetraodonTetraodon nigroviridisTetraodontidaeVertebrataThe proopiomelanocortin gene (POMC) encodes several bioactive peptides, including adrenocorticotropin hormone, α-, β-, and γ-melanocyte-stimulating hormone, and the opioid peptide β-endorphin, which play key roles in vertebrate physiology. In the human, mouse, and chicken genomes, there is only one POMC gene. By searching public genome projects, we have found that Tetraodon (Tetraodon nigroviridis), Fugu (Takifugu rubripes), and zebrafish (Danio rerio) possess two POMC genes, which we called POMCα and POMCβ, and we present phylogenetic and mapping evidence that these paralogue genes originated in the whole-genome duplication specific to the teleost lineage over 300 MYA. In addition, we present evidence for two types of subfunction partitioning between the paralogues. First, in situ hybridization experiments indicate that the expression domains of the ancestral POMC gene have been subfunctionalized in Tetraodon, with POMCα expressed in the nucleus lateralis tuberis of the hypothalamus, as well as in the rostral pars distalis and pars intermedia (PI) of the pituitary, whereas POMCβ is expressed in the preoptic area of the brain and weakly in the pituitary PI. Second, POMCβ genes have a β-endorphin segment that lacks the consensus opioid signal and seems to be under neutral evolution in tetraodontids, whereas POMCα genes possess well-conserved peptide regions. Thus, POMC paralogues have experienced subfunctionalization of both expression and peptide domains during teleost evolution. The study of regulatory regions of fish POMC genes might shed light on the mechanisms of enhancer partitioning between duplicate genes, as well as the roles of POMC-derived peptides in fish physiology.Fil:Rubinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_07374038_v22_n12_p2417_DeSouzaMol. Biol. Evol. 2005;22(12):2417-2427reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-10-23T11:18:29Zpaperaa:paper_07374038_v22_n12_p2417_DeSouzaInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-23 11:18:30.06Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
title Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
spellingShingle Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
De Souza, F.S.J.
β-endorphin
Evolution
POMC
Subfunctionalization
Teleosts
Tetraodon
opiate
proopiomelanocortin
article
gene duplication
gene mapping
hypophysis
hypothalamus nucleus
in situ hybridization
molecular evolution
nonhuman
nucleotide sequence
phylogeny
preoptic area
protein domain
protein expression
protein function
signal transduction
teleost
Amino Acid Sequence
Animals
Evolution, Molecular
Fishes
Gene Duplication
Molecular Sequence Data
Phylogeny
Pro-Opiomelanocortin
Sequence Alignment
Tetraodontiformes
Zebrafish
Danio rerio
Takifugu
Takifugu rubripes
Teleostei
Tetraodon
Tetraodon nigroviridis
Tetraodontidae
Vertebrata
title_short Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
title_full Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
title_fullStr Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
title_full_unstemmed Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
title_sort Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
dc.creator.none.fl_str_mv De Souza, F.S.J.
Bumaschny, V.F.
Low, M.J.
Rubinstein, M.
author De Souza, F.S.J.
author_facet De Souza, F.S.J.
Bumaschny, V.F.
Low, M.J.
Rubinstein, M.
author_role author
author2 Bumaschny, V.F.
Low, M.J.
Rubinstein, M.
author2_role author
author
author
dc.subject.none.fl_str_mv β-endorphin
Evolution
POMC
Subfunctionalization
Teleosts
Tetraodon
opiate
proopiomelanocortin
article
gene duplication
gene mapping
hypophysis
hypothalamus nucleus
in situ hybridization
molecular evolution
nonhuman
nucleotide sequence
phylogeny
preoptic area
protein domain
protein expression
protein function
signal transduction
teleost
Amino Acid Sequence
Animals
Evolution, Molecular
Fishes
Gene Duplication
Molecular Sequence Data
Phylogeny
Pro-Opiomelanocortin
Sequence Alignment
Tetraodontiformes
Zebrafish
Danio rerio
Takifugu
Takifugu rubripes
Teleostei
Tetraodon
Tetraodon nigroviridis
Tetraodontidae
Vertebrata
topic β-endorphin
Evolution
POMC
Subfunctionalization
Teleosts
Tetraodon
opiate
proopiomelanocortin
article
gene duplication
gene mapping
hypophysis
hypothalamus nucleus
in situ hybridization
molecular evolution
nonhuman
nucleotide sequence
phylogeny
preoptic area
protein domain
protein expression
protein function
signal transduction
teleost
Amino Acid Sequence
Animals
Evolution, Molecular
Fishes
Gene Duplication
Molecular Sequence Data
Phylogeny
Pro-Opiomelanocortin
Sequence Alignment
Tetraodontiformes
Zebrafish
Danio rerio
Takifugu
Takifugu rubripes
Teleostei
Tetraodon
Tetraodon nigroviridis
Tetraodontidae
Vertebrata
dc.description.none.fl_txt_mv The proopiomelanocortin gene (POMC) encodes several bioactive peptides, including adrenocorticotropin hormone, α-, β-, and γ-melanocyte-stimulating hormone, and the opioid peptide β-endorphin, which play key roles in vertebrate physiology. In the human, mouse, and chicken genomes, there is only one POMC gene. By searching public genome projects, we have found that Tetraodon (Tetraodon nigroviridis), Fugu (Takifugu rubripes), and zebrafish (Danio rerio) possess two POMC genes, which we called POMCα and POMCβ, and we present phylogenetic and mapping evidence that these paralogue genes originated in the whole-genome duplication specific to the teleost lineage over 300 MYA. In addition, we present evidence for two types of subfunction partitioning between the paralogues. First, in situ hybridization experiments indicate that the expression domains of the ancestral POMC gene have been subfunctionalized in Tetraodon, with POMCα expressed in the nucleus lateralis tuberis of the hypothalamus, as well as in the rostral pars distalis and pars intermedia (PI) of the pituitary, whereas POMCβ is expressed in the preoptic area of the brain and weakly in the pituitary PI. Second, POMCβ genes have a β-endorphin segment that lacks the consensus opioid signal and seems to be under neutral evolution in tetraodontids, whereas POMCα genes possess well-conserved peptide regions. Thus, POMC paralogues have experienced subfunctionalization of both expression and peptide domains during teleost evolution. The study of regulatory regions of fish POMC genes might shed light on the mechanisms of enhancer partitioning between duplicate genes, as well as the roles of POMC-derived peptides in fish physiology.
Fil:Rubinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description The proopiomelanocortin gene (POMC) encodes several bioactive peptides, including adrenocorticotropin hormone, α-, β-, and γ-melanocyte-stimulating hormone, and the opioid peptide β-endorphin, which play key roles in vertebrate physiology. In the human, mouse, and chicken genomes, there is only one POMC gene. By searching public genome projects, we have found that Tetraodon (Tetraodon nigroviridis), Fugu (Takifugu rubripes), and zebrafish (Danio rerio) possess two POMC genes, which we called POMCα and POMCβ, and we present phylogenetic and mapping evidence that these paralogue genes originated in the whole-genome duplication specific to the teleost lineage over 300 MYA. In addition, we present evidence for two types of subfunction partitioning between the paralogues. First, in situ hybridization experiments indicate that the expression domains of the ancestral POMC gene have been subfunctionalized in Tetraodon, with POMCα expressed in the nucleus lateralis tuberis of the hypothalamus, as well as in the rostral pars distalis and pars intermedia (PI) of the pituitary, whereas POMCβ is expressed in the preoptic area of the brain and weakly in the pituitary PI. Second, POMCβ genes have a β-endorphin segment that lacks the consensus opioid signal and seems to be under neutral evolution in tetraodontids, whereas POMCα genes possess well-conserved peptide regions. Thus, POMC paralogues have experienced subfunctionalization of both expression and peptide domains during teleost evolution. The study of regulatory regions of fish POMC genes might shed light on the mechanisms of enhancer partitioning between duplicate genes, as well as the roles of POMC-derived peptides in fish physiology.
publishDate 2005
dc.date.none.fl_str_mv 2005
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_07374038_v22_n12_p2417_DeSouza
url http://hdl.handle.net/20.500.12110/paper_07374038_v22_n12_p2417_DeSouza
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Mol. Biol. Evol. 2005;22(12):2417-2427
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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