Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit
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 stra...
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todo:paper_00220957_v61_n14_p3935_Alleva2023-10-03T14:26:14Z Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit Alleva, K. Marquez, M. Villarreal, N. Mut, P. Bustamante, C. Bellati, J. Martínez, G. Civello, M. Amodeo, G. 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 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00220957_v61_n14_p3935_Alleva |
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 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 |
spellingShingle |
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 Alleva, K. Marquez, M. Villarreal, N. Mut, P. Bustamante, C. Bellati, J. Martínez, G. Civello, M. Amodeo, G. Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit |
topic_facet |
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 |
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). |
format |
JOUR |
author |
Alleva, K. Marquez, M. Villarreal, N. Mut, P. Bustamante, C. Bellati, J. Martínez, G. Civello, M. Amodeo, G. |
author_facet |
Alleva, K. Marquez, M. Villarreal, N. Mut, P. Bustamante, C. Bellati, J. Martínez, G. Civello, M. Amodeo, G. |
author_sort |
Alleva, K. |
title |
Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit |
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 |
url |
http://hdl.handle.net/20.500.12110/paper_00220957_v61_n14_p3935_Alleva |
work_keys_str_mv |
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