New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible
Aquaporins (AQPs) represent a family of channel proteins that transport water and/or small solutes across cell membranes in the three domains of life. In all previous phylogenetic analysis of aquaporin, trees constructed using proteins with very low amino acid identity (< 15%) were incongruent wi...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781119_v503_n1_p165_Soto http://hdl.handle.net/20.500.12110/paper_03781119_v503_n1_p165_Soto |
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paper:paper_03781119_v503_n1_p165_Soto2023-06-08T15:39:16Z New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible Soto, Gabriela Cynthia Muschietti, Jorge P. Ayub, Nicolás Daniel Aquaporin Evolution Gene transfer Orthologs amino acid aquaporin aquaporin 1 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 8 aquaporin 9 bacterial glycerol transporter carrier proteins and binding proteins unclassified drug amino acid analysis Arabidopsis eudicot flowering Gallus gallus gene cluster gene transfer grain Hevea brasiliensis Hordeum human letter molecular evolution monocot mouse nomenclature nonhuman nucleotide sequence orthology phylogenetic tree plant genetics Populus trichocarpa priority journal protein analysis Rattus norvergicus Ricinus communis sequence analysis soybean vertebrate zebra fish Amino Acid Sequence Animals Aquaporins Biological Evolution Evolution, Molecular Humans Molecular Sequence Data Phylogeny Plants Vertebrates Water Animalia Arabidopsis thaliana Dicotyledoneae Homo sapiens Liliopsida Magnoliophyta Pips Pisces Tetrapoda Vertebrata Aquaporins (AQPs) represent a family of channel proteins that transport water and/or small solutes across cell membranes in the three domains of life. In all previous phylogenetic analysis of aquaporin, trees constructed using proteins with very low amino acid identity (< 15%) were incongruent with rRNA data. In this work, restricting the evolutionary study of aquaporins to proteins with high amino acid identity (> 25%), we showed congruence between AQPs and organismal trees. On the basis of this analysis, we defined 19 orthologous gene clusters in flowering plant species (3 PIP-like, 7 TIP-like, 6 NIP-like and 3 SIP-like). We described specific conserved motifs for each subfamily and each cluster, which were used to develop a method for automatic classification. Analysis of amino acid identity between orthologous monocotyledon and dicotyledon AQPs from each cluster, suggested that PIPs are under high evolutionary constraint. The phylogenetic analysis allowed us the assignment of orthologous aquaporins for very distant animal lineages (tetrapods-fishes). We also demonstrated that the location of all vertebrate AQPs in the ortholog clusters could be predicted by comparing their amino acid identity with human AQPs. We defined four AQP subfamilies in animals: AQP1-like, AQP8-like, AQP3-like and AQP11-like. Phylogenetic analysis showed that the four animal AQPs subfamilies are related with PIP-like, TIP-like, NIP-like and SIP-like subfamilies, respectively. Thus, this analysis would allow the prediction of individual AQPs function on the basis of orthologous genes from Arabidopsis thaliana and Homo sapiens. © 2012 Elsevier B.V. Fil:Soto, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Muschietti, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ayub, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781119_v503_n1_p165_Soto http://hdl.handle.net/20.500.12110/paper_03781119_v503_n1_p165_Soto |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Aquaporin Evolution Gene transfer Orthologs amino acid aquaporin aquaporin 1 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 8 aquaporin 9 bacterial glycerol transporter carrier proteins and binding proteins unclassified drug amino acid analysis Arabidopsis eudicot flowering Gallus gallus gene cluster gene transfer grain Hevea brasiliensis Hordeum human letter molecular evolution monocot mouse nomenclature nonhuman nucleotide sequence orthology phylogenetic tree plant genetics Populus trichocarpa priority journal protein analysis Rattus norvergicus Ricinus communis sequence analysis soybean vertebrate zebra fish Amino Acid Sequence Animals Aquaporins Biological Evolution Evolution, Molecular Humans Molecular Sequence Data Phylogeny Plants Vertebrates Water Animalia Arabidopsis thaliana Dicotyledoneae Homo sapiens Liliopsida Magnoliophyta Pips Pisces Tetrapoda Vertebrata |
spellingShingle |
Aquaporin Evolution Gene transfer Orthologs amino acid aquaporin aquaporin 1 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 8 aquaporin 9 bacterial glycerol transporter carrier proteins and binding proteins unclassified drug amino acid analysis Arabidopsis eudicot flowering Gallus gallus gene cluster gene transfer grain Hevea brasiliensis Hordeum human letter molecular evolution monocot mouse nomenclature nonhuman nucleotide sequence orthology phylogenetic tree plant genetics Populus trichocarpa priority journal protein analysis Rattus norvergicus Ricinus communis sequence analysis soybean vertebrate zebra fish Amino Acid Sequence Animals Aquaporins Biological Evolution Evolution, Molecular Humans Molecular Sequence Data Phylogeny Plants Vertebrates Water Animalia Arabidopsis thaliana Dicotyledoneae Homo sapiens Liliopsida Magnoliophyta Pips Pisces Tetrapoda Vertebrata Soto, Gabriela Cynthia Muschietti, Jorge P. Ayub, Nicolás Daniel New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible |
topic_facet |
Aquaporin Evolution Gene transfer Orthologs amino acid aquaporin aquaporin 1 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 8 aquaporin 9 bacterial glycerol transporter carrier proteins and binding proteins unclassified drug amino acid analysis Arabidopsis eudicot flowering Gallus gallus gene cluster gene transfer grain Hevea brasiliensis Hordeum human letter molecular evolution monocot mouse nomenclature nonhuman nucleotide sequence orthology phylogenetic tree plant genetics Populus trichocarpa priority journal protein analysis Rattus norvergicus Ricinus communis sequence analysis soybean vertebrate zebra fish Amino Acid Sequence Animals Aquaporins Biological Evolution Evolution, Molecular Humans Molecular Sequence Data Phylogeny Plants Vertebrates Water Animalia Arabidopsis thaliana Dicotyledoneae Homo sapiens Liliopsida Magnoliophyta Pips Pisces Tetrapoda Vertebrata |
description |
Aquaporins (AQPs) represent a family of channel proteins that transport water and/or small solutes across cell membranes in the three domains of life. In all previous phylogenetic analysis of aquaporin, trees constructed using proteins with very low amino acid identity (< 15%) were incongruent with rRNA data. In this work, restricting the evolutionary study of aquaporins to proteins with high amino acid identity (> 25%), we showed congruence between AQPs and organismal trees. On the basis of this analysis, we defined 19 orthologous gene clusters in flowering plant species (3 PIP-like, 7 TIP-like, 6 NIP-like and 3 SIP-like). We described specific conserved motifs for each subfamily and each cluster, which were used to develop a method for automatic classification. Analysis of amino acid identity between orthologous monocotyledon and dicotyledon AQPs from each cluster, suggested that PIPs are under high evolutionary constraint. The phylogenetic analysis allowed us the assignment of orthologous aquaporins for very distant animal lineages (tetrapods-fishes). We also demonstrated that the location of all vertebrate AQPs in the ortholog clusters could be predicted by comparing their amino acid identity with human AQPs. We defined four AQP subfamilies in animals: AQP1-like, AQP8-like, AQP3-like and AQP11-like. Phylogenetic analysis showed that the four animal AQPs subfamilies are related with PIP-like, TIP-like, NIP-like and SIP-like subfamilies, respectively. Thus, this analysis would allow the prediction of individual AQPs function on the basis of orthologous genes from Arabidopsis thaliana and Homo sapiens. © 2012 Elsevier B.V. |
author |
Soto, Gabriela Cynthia Muschietti, Jorge P. Ayub, Nicolás Daniel |
author_facet |
Soto, Gabriela Cynthia Muschietti, Jorge P. Ayub, Nicolás Daniel |
author_sort |
Soto, Gabriela Cynthia |
title |
New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible |
title_short |
New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible |
title_full |
New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible |
title_fullStr |
New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible |
title_full_unstemmed |
New insight into the evolution of aquaporins from flowering plants and vertebrates: Orthologous identification and functional transfer is possible |
title_sort |
new insight into the evolution of aquaporins from flowering plants and vertebrates: orthologous identification and functional transfer is possible |
publishDate |
2012 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781119_v503_n1_p165_Soto http://hdl.handle.net/20.500.12110/paper_03781119_v503_n1_p165_Soto |
work_keys_str_mv |
AT sotogabrielacynthia newinsightintotheevolutionofaquaporinsfromfloweringplantsandvertebratesorthologousidentificationandfunctionaltransferispossible AT muschiettijorgep newinsightintotheevolutionofaquaporinsfromfloweringplantsandvertebratesorthologousidentificationandfunctionaltransferispossible AT ayubnicolasdaniel newinsightintotheevolutionofaquaporinsfromfloweringplantsandvertebratesorthologousidentificationandfunctionaltransferispossible |
_version_ |
1768544184210292736 |