Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes
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...
Guardado en:
Autores principales: | , , , |
---|---|
Formato: | Artículo publishedVersion |
Publicado: |
2005
|
Materias: | |
Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_07374038_v22_n12_p2417_DeSouza https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_07374038_v22_n12_p2417_DeSouza_oai |
Aporte de: |
id |
I28-R145-paper_07374038_v22_n12_p2417_DeSouza_oai |
---|---|
record_format |
dspace |
spelling |
I28-R145-paper_07374038_v22_n12_p2417_DeSouza_oai2024-08-16 De Souza, F.S.J. Bumaschny, V.F. Low, M.J. Rubinstein, M. 2005 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. application/pdf http://hdl.handle.net/20.500.12110/paper_07374038_v22_n12_p2417_DeSouza info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Mol. Biol. Evol. 2005;22(12):2417-2427 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 Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_07374038_v22_n12_p2417_DeSouza_oai |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-145 |
collection |
Repositorio Digital de la Universidad de Buenos Aires (UBA) |
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 |
spellingShingle |
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 De Souza, F.S.J. Bumaschny, V.F. Low, M.J. Rubinstein, M. Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes |
topic_facet |
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 |
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. |
format |
Artículo Artículo publishedVersion |
author |
De Souza, F.S.J. Bumaschny, V.F. Low, M.J. Rubinstein, M. |
author_facet |
De Souza, F.S.J. Bumaschny, V.F. Low, M.J. Rubinstein, M. |
author_sort |
De Souza, F.S.J. |
title |
Subfunctionalization of expression and peptide domains following the ancient duplication of the proopiomelanocortin gene in teleost fishes |
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 |
publishDate |
2005 |
url |
http://hdl.handle.net/20.500.12110/paper_07374038_v22_n12_p2417_DeSouza https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_07374038_v22_n12_p2417_DeSouza_oai |
work_keys_str_mv |
AT desouzafsj subfunctionalizationofexpressionandpeptidedomainsfollowingtheancientduplicationoftheproopiomelanocortingeneinteleostfishes AT bumaschnyvf subfunctionalizationofexpressionandpeptidedomainsfollowingtheancientduplicationoftheproopiomelanocortingeneinteleostfishes AT lowmj subfunctionalizationofexpressionandpeptidedomainsfollowingtheancientduplicationoftheproopiomelanocortingeneinteleostfishes AT rubinsteinm subfunctionalizationofexpressionandpeptidedomainsfollowingtheancientduplicationoftheproopiomelanocortingeneinteleostfishes |
_version_ |
1809356911210921984 |