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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_07374038_v22_n12_p2417_DeSouza
Ver los metadatos del registro completo
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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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1846784880950640640 |
score |
12.982451 |