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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_00220957_v61_n14_p3935_Alleva
Ver los metadatos del registro completo
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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 |
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Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
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UBA-FCEN |
repository.name.fl_str_mv |
Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
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