Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit

Autores
Alleva, K.; Marquez, M.; Villarreal, N.; Mut, P.; Bustamante, C.; Bellati, J.; Martínez, G.; Civello, M.; Amodeo, G.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In strawberry, the putative participation of aquaporins should be considered during fruit ripening. Furthermore, the availability of different firmness cultivars in this non-climacteric fruit is a very useful tool to determine their involvement in softening. In a previous work, the cloning of a strawberry fruit-specific aquaporin, FaPIP1;1, which showed an expression profile associated with fruit ripening was reported. Here, FaPIP2;1, an aquaporin subtype of PIP2 was cloned and its functional characterization in Xenopus oocytes determined. The FaPIP2;1 gene encodes a water channel with high water permeability (Pf) that is regulated by cytosolic pH. Interestingly, the co-expression of both FaPIP subtypes resulted in an enhancement of water permeability, showing Pf values that exceeds their individual contribution. The expression pattern of both aquaporin subtypes in two cultivars with contrasting fruit firmness showed that the firmer cultivar (Camarosa) has a higher accumulation of FaPIP1 and FaPIP2 mRNAs during fruit ripening when compared with the softer cultivar (Toyonoka). In conclusion, not only FaPIP aquaporins showed an expression pattern associated with fruit firmness but it was also shown that the enhancement of water transfer through the plasma membrane is coupled to the presence/absence of the co-expression of both subtypes. © 2010 The Author(s).
Fil:Mut, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
J. Exp. Bot. 2010;61(14):3935-3945
Materia
Aquaporin
fruit ripening
PIP
strawberry
water transport
aquaporin
complementary DNA
vegetable protein
water
aquaporin
vegetable protein
amino acid sequence
animal
article
cell membrane
chemistry
fruit
genetics
metabolism
molecular cloning
molecular genetics
permeability
strawberry
Xenopus laevis
Fragaria
fruit
metabolism
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
Fragaria x ananassa
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
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_00220957_v61_n14_p3935_Alleva

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oai_identifier_str paperaa:paper_00220957_v61_n14_p3935_Alleva
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruitAlleva, K.Marquez, M.Villarreal, N.Mut, P.Bustamante, C.Bellati, J.Martínez, G.Civello, M.Amodeo, G.Aquaporinfruit ripeningPIPstrawberrywater transportaquaporincomplementary DNAvegetable proteinwateraquaporinvegetable proteinamino acid sequenceanimalarticlecell membranechemistryfruitgeneticsmetabolismmolecular cloningmolecular geneticspermeabilitystrawberryXenopus laevisFragariafruitmetabolismAmino Acid SequenceAnimalsAquaporinsCell MembraneCloning, MolecularDNA, ComplementaryFragariaFruitMolecular Sequence DataPermeabilityPlant ProteinsWaterXenopus laevisFragaria x ananassaAmino Acid SequenceAnimalsAquaporinsCell MembraneCloning, MolecularDNA, ComplementaryFragariaFruitMolecular Sequence DataPermeabilityPlant ProteinsWaterXenopus laevisIn strawberry, the putative participation of aquaporins should be considered during fruit ripening. Furthermore, the availability of different firmness cultivars in this non-climacteric fruit is a very useful tool to determine their involvement in softening. In a previous work, the cloning of a strawberry fruit-specific aquaporin, FaPIP1;1, which showed an expression profile associated with fruit ripening was reported. Here, FaPIP2;1, an aquaporin subtype of PIP2 was cloned and its functional characterization in Xenopus oocytes determined. The FaPIP2;1 gene encodes a water channel with high water permeability (Pf) that is regulated by cytosolic pH. Interestingly, the co-expression of both FaPIP subtypes resulted in an enhancement of water permeability, showing Pf values that exceeds their individual contribution. The expression pattern of both aquaporin subtypes in two cultivars with contrasting fruit firmness showed that the firmer cultivar (Camarosa) has a higher accumulation of FaPIP1 and FaPIP2 mRNAs during fruit ripening when compared with the softer cultivar (Toyonoka). In conclusion, not only FaPIP aquaporins showed an expression pattern associated with fruit firmness but it was also shown that the enhancement of water transfer through the plasma membrane is coupled to the presence/absence of the co-expression of both subtypes. © 2010 The Author(s).Fil:Mut, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2010info: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_00220957_v61_n14_p3935_AllevaJ. Exp. Bot. 2010;61(14):3935-3945reponame: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/ar2025-09-29T13:43:05Zpaperaa:paper_00220957_v61_n14_p3935_AllevaInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:07.011Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
title Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
spellingShingle Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
Alleva, K.
Aquaporin
fruit ripening
PIP
strawberry
water transport
aquaporin
complementary DNA
vegetable protein
water
aquaporin
vegetable protein
amino acid sequence
animal
article
cell membrane
chemistry
fruit
genetics
metabolism
molecular cloning
molecular genetics
permeability
strawberry
Xenopus laevis
Fragaria
fruit
metabolism
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
Fragaria x ananassa
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
title_short Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
title_full Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
title_fullStr Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
title_full_unstemmed Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
title_sort Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
dc.creator.none.fl_str_mv Alleva, K.
Marquez, M.
Villarreal, N.
Mut, P.
Bustamante, C.
Bellati, J.
Martínez, G.
Civello, M.
Amodeo, G.
author Alleva, K.
author_facet Alleva, K.
Marquez, M.
Villarreal, N.
Mut, P.
Bustamante, C.
Bellati, J.
Martínez, G.
Civello, M.
Amodeo, G.
author_role author
author2 Marquez, M.
Villarreal, N.
Mut, P.
Bustamante, C.
Bellati, J.
Martínez, G.
Civello, M.
Amodeo, G.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Aquaporin
fruit ripening
PIP
strawberry
water transport
aquaporin
complementary DNA
vegetable protein
water
aquaporin
vegetable protein
amino acid sequence
animal
article
cell membrane
chemistry
fruit
genetics
metabolism
molecular cloning
molecular genetics
permeability
strawberry
Xenopus laevis
Fragaria
fruit
metabolism
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
Fragaria x ananassa
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
topic Aquaporin
fruit ripening
PIP
strawberry
water transport
aquaporin
complementary DNA
vegetable protein
water
aquaporin
vegetable protein
amino acid sequence
animal
article
cell membrane
chemistry
fruit
genetics
metabolism
molecular cloning
molecular genetics
permeability
strawberry
Xenopus laevis
Fragaria
fruit
metabolism
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
Fragaria x ananassa
Amino Acid Sequence
Animals
Aquaporins
Cell Membrane
Cloning, Molecular
DNA, Complementary
Fragaria
Fruit
Molecular Sequence Data
Permeability
Plant Proteins
Water
Xenopus laevis
dc.description.none.fl_txt_mv In strawberry, the putative participation of aquaporins should be considered during fruit ripening. Furthermore, the availability of different firmness cultivars in this non-climacteric fruit is a very useful tool to determine their involvement in softening. In a previous work, the cloning of a strawberry fruit-specific aquaporin, FaPIP1;1, which showed an expression profile associated with fruit ripening was reported. Here, FaPIP2;1, an aquaporin subtype of PIP2 was cloned and its functional characterization in Xenopus oocytes determined. The FaPIP2;1 gene encodes a water channel with high water permeability (Pf) that is regulated by cytosolic pH. Interestingly, the co-expression of both FaPIP subtypes resulted in an enhancement of water permeability, showing Pf values that exceeds their individual contribution. The expression pattern of both aquaporin subtypes in two cultivars with contrasting fruit firmness showed that the firmer cultivar (Camarosa) has a higher accumulation of FaPIP1 and FaPIP2 mRNAs during fruit ripening when compared with the softer cultivar (Toyonoka). In conclusion, not only FaPIP aquaporins showed an expression pattern associated with fruit firmness but it was also shown that the enhancement of water transfer through the plasma membrane is coupled to the presence/absence of the co-expression of both subtypes. © 2010 The Author(s).
Fil:Mut, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description In strawberry, the putative participation of aquaporins should be considered during fruit ripening. Furthermore, the availability of different firmness cultivars in this non-climacteric fruit is a very useful tool to determine their involvement in softening. In a previous work, the cloning of a strawberry fruit-specific aquaporin, FaPIP1;1, which showed an expression profile associated with fruit ripening was reported. Here, FaPIP2;1, an aquaporin subtype of PIP2 was cloned and its functional characterization in Xenopus oocytes determined. The FaPIP2;1 gene encodes a water channel with high water permeability (Pf) that is regulated by cytosolic pH. Interestingly, the co-expression of both FaPIP subtypes resulted in an enhancement of water permeability, showing Pf values that exceeds their individual contribution. The expression pattern of both aquaporin subtypes in two cultivars with contrasting fruit firmness showed that the firmer cultivar (Camarosa) has a higher accumulation of FaPIP1 and FaPIP2 mRNAs during fruit ripening when compared with the softer cultivar (Toyonoka). In conclusion, not only FaPIP aquaporins showed an expression pattern associated with fruit firmness but it was also shown that the enhancement of water transfer through the plasma membrane is coupled to the presence/absence of the co-expression of both subtypes. © 2010 The Author(s).
publishDate 2010
dc.date.none.fl_str_mv 2010
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_00220957_v61_n14_p3935_Alleva
url http://hdl.handle.net/20.500.12110/paper_00220957_v61_n14_p3935_Alleva
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 J. Exp. Bot. 2010;61(14):3935-3945
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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