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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Autores principales: Soto, Gabriela Cynthia, Muschietti, Jorge P., Ayub, Nicolás Daniel
Publicado: 2012
Materias:
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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spelling 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
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AT muschiettijorgep newinsightintotheevolutionofaquaporinsfromfloweringplantsandvertebratesorthologousidentificationandfunctionaltransferispossible
AT ayubnicolasdaniel newinsightintotheevolutionofaquaporinsfromfloweringplantsandvertebratesorthologousidentificationandfunctionaltransferispossible
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