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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Autor principal: Mut, Paula
Publicado: 2010
Materias:
PIP
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00220957_v61_n14_p3935_Alleva
http://hdl.handle.net/20.500.12110/paper_00220957_v61_n14_p3935_Alleva
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spelling paper:paper_00220957_v61_n14_p3935_Alleva2023-06-08T14:45:42Z Cloning, functional characterization, and co-expression studies of a novel aquaporin (FaPIP2;1) of strawberry fruit Mut, Paula 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. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00220957_v61_n14_p3935_Alleva 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
Mut, Paula
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).
author Mut, Paula
author_facet Mut, Paula
author_sort Mut, Paula
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
publishDate 2010
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00220957_v61_n14_p3935_Alleva
http://hdl.handle.net/20.500.12110/paper_00220957_v61_n14_p3935_Alleva
work_keys_str_mv AT mutpaula cloningfunctionalcharacterizationandcoexpressionstudiesofanovelaquaporinfapip21ofstrawberryfruit
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