Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos

The aim of this study was to characterize the dehydrin content in mature embryos of two quinoa cultivars, Sajama and Baer La Unión. Cultivar Sajama grows at 3600-4000 m altitude and is adapted to the very arid conditions characteristic of the salty soils of the Bolivian Altiplano, with less than 250...

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Autores principales:	Carjuzaa, P., Castellión, M., Distéfano, A.J., Del Vas, M., Maldonado, S.
Formato:	JOUR
Materias:	Chenopodium quinoa Dehydrin Environment In situ immunolocalization Quinoa cultivar Western blot analysis dehydrin proteins, plant vegetable protein article cell fractionation meristem metabolism plant seed prenatal development protein transport ultrastructure Western blotting Blotting, Western Meristem Plant Proteins Protein Transport Seeds Subcellular Fractions
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_0033183X_v233_n1-2_p149_Carjuzaa
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_0033183X_v233_n1-2_p149_Carjuzaa
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spelling	todo:paper_0033183X_v233_n1-2_p149_Carjuzaa2023-10-03T14:45:31Z Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos Carjuzaa, P. Castellión, M. Distéfano, A.J. Del Vas, M. Maldonado, S. Chenopodium quinoa Dehydrin Environment In situ immunolocalization Quinoa cultivar Western blot analysis dehydrin proteins, plant vegetable protein article cell fractionation Chenopodium quinoa meristem metabolism plant seed prenatal development protein transport ultrastructure Western blotting Blotting, Western Chenopodium quinoa Meristem Plant Proteins Protein Transport Seeds Subcellular Fractions Chenopodium quinoa The aim of this study was to characterize the dehydrin content in mature embryos of two quinoa cultivars, Sajama and Baer La Unión. Cultivar Sajama grows at 3600-4000 m altitude and is adapted to the very arid conditions characteristic of the salty soils of the Bolivian Altiplano, with less than 250 mm of annual rain and a minimum temperature of -1 °C. Cultivar Baer La Unión grows at sea-level regions of central Chile and is adapted to more humid conditions (800 to 1500 mm of annual rain), fertile soils, and temperatures above 5 °C. Western blot analysis of embryo tissues from plants growing under controlled greenhouse conditions clearly revealed the presence of several dehydrin bands (at molecular masses of approximately 30, 32, 50, and 55 kDa), which were common to both cultivars, although the amount of the 30 and 32 kDa bands differed. Nevertheless, when grains originated from their respective natural environments, three extra bands (at molecular masses of approximately 34, 38, and 40 kDa), which were hardly visible in Sajama, and another weak band (at a molecular mass of approximately 28 kDa) were evident in Baer La Unión. In situ immunolocalization microscopy detected dehydrin-like proteins in all axis and cotyledon tissues. At the subcellular level, dehydrins were detected in the plasma membrane, cytoplasm and nucleus. In the cytoplasm, dehydrins were found associated with mitochondria, rough endoplasmic reticulum cisternae, and proplastid membranes. The presence of dehydrins was also recognized in the matrix of protein bodies. In the nucleus, dehydrins were associated with the euchromatin. Upon examining dehydrin composition and subcellular localization in two quinoa cultivars belonging to highly contrasting environments, we conclude that most dehydrins detected here were constitutive components of the quinoa seed developmental program, but some of them (specially the 34, 38, and 40 kDa bands) may reflect quantitative molecular differences associated with the adaptation of both cultivars to contrasting environmental conditions. © 2008 Springer-Verlag. Fil:Castellión, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Distéfano, A.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del Vas, M. 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_0033183X_v233_n1-2_p149_Carjuzaa
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Chenopodium quinoa Dehydrin Environment In situ immunolocalization Quinoa cultivar Western blot analysis dehydrin proteins, plant vegetable protein article cell fractionation Chenopodium quinoa meristem metabolism plant seed prenatal development protein transport ultrastructure Western blotting Blotting, Western Chenopodium quinoa Meristem Plant Proteins Protein Transport Seeds Subcellular Fractions Chenopodium quinoa
spellingShingle	Chenopodium quinoa Dehydrin Environment In situ immunolocalization Quinoa cultivar Western blot analysis dehydrin proteins, plant vegetable protein article cell fractionation Chenopodium quinoa meristem metabolism plant seed prenatal development protein transport ultrastructure Western blotting Blotting, Western Chenopodium quinoa Meristem Plant Proteins Protein Transport Seeds Subcellular Fractions Chenopodium quinoa Carjuzaa, P. Castellión, M. Distéfano, A.J. Del Vas, M. Maldonado, S. Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos
topic_facet	Chenopodium quinoa Dehydrin Environment In situ immunolocalization Quinoa cultivar Western blot analysis dehydrin proteins, plant vegetable protein article cell fractionation Chenopodium quinoa meristem metabolism plant seed prenatal development protein transport ultrastructure Western blotting Blotting, Western Chenopodium quinoa Meristem Plant Proteins Protein Transport Seeds Subcellular Fractions Chenopodium quinoa
description	The aim of this study was to characterize the dehydrin content in mature embryos of two quinoa cultivars, Sajama and Baer La Unión. Cultivar Sajama grows at 3600-4000 m altitude and is adapted to the very arid conditions characteristic of the salty soils of the Bolivian Altiplano, with less than 250 mm of annual rain and a minimum temperature of -1 °C. Cultivar Baer La Unión grows at sea-level regions of central Chile and is adapted to more humid conditions (800 to 1500 mm of annual rain), fertile soils, and temperatures above 5 °C. Western blot analysis of embryo tissues from plants growing under controlled greenhouse conditions clearly revealed the presence of several dehydrin bands (at molecular masses of approximately 30, 32, 50, and 55 kDa), which were common to both cultivars, although the amount of the 30 and 32 kDa bands differed. Nevertheless, when grains originated from their respective natural environments, three extra bands (at molecular masses of approximately 34, 38, and 40 kDa), which were hardly visible in Sajama, and another weak band (at a molecular mass of approximately 28 kDa) were evident in Baer La Unión. In situ immunolocalization microscopy detected dehydrin-like proteins in all axis and cotyledon tissues. At the subcellular level, dehydrins were detected in the plasma membrane, cytoplasm and nucleus. In the cytoplasm, dehydrins were found associated with mitochondria, rough endoplasmic reticulum cisternae, and proplastid membranes. The presence of dehydrins was also recognized in the matrix of protein bodies. In the nucleus, dehydrins were associated with the euchromatin. Upon examining dehydrin composition and subcellular localization in two quinoa cultivars belonging to highly contrasting environments, we conclude that most dehydrins detected here were constitutive components of the quinoa seed developmental program, but some of them (specially the 34, 38, and 40 kDa bands) may reflect quantitative molecular differences associated with the adaptation of both cultivars to contrasting environmental conditions. © 2008 Springer-Verlag.
format	JOUR
author	Carjuzaa, P. Castellión, M. Distéfano, A.J. Del Vas, M. Maldonado, S.
author_facet	Carjuzaa, P. Castellión, M. Distéfano, A.J. Del Vas, M. Maldonado, S.
author_sort	Carjuzaa, P.
title	Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos
title_short	Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos
title_full	Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos
title_fullStr	Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos
title_full_unstemmed	Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos
title_sort	detection and subcellular localization of dehydrin-like proteins in quinoa (chenopodium quinoa willd.) embryos
url	http://hdl.handle.net/20.500.12110/paper_0033183X_v233_n1-2_p149_Carjuzaa
work_keys_str_mv	AT carjuzaap detectionandsubcellularlocalizationofdehydrinlikeproteinsinquinoachenopodiumquinoawilldembryos AT castellionm detectionandsubcellularlocalizationofdehydrinlikeproteinsinquinoachenopodiumquinoawilldembryos AT distefanoaj detectionandsubcellularlocalizationofdehydrinlikeproteinsinquinoachenopodiumquinoawilldembryos AT delvasm detectionandsubcellularlocalizationofdehydrinlikeproteinsinquinoachenopodiumquinoawilldembryos AT maldonados detectionandsubcellularlocalizationofdehydrinlikeproteinsinquinoachenopodiumquinoawilldembryos
_version_	1782023731712884736

Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos

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