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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2008
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| LEADER | 15826caa a22012977a 4500 | ||
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| 001 | PAPER-5734 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203524.0 | ||
| 008 | 190411s2008 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-51749092625 | |
| 024 | 7 | |2 cas |a dehydrin proteins, plant, 134711-03-8; Plant Proteins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a PROTA | ||
| 100 | 1 | |a Carjuzaa, P. | |
| 245 | 1 | 0 | |a Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos |
| 260 | |c 2008 | ||
| 270 | 1 | 0 | |m Maldonado, S.; Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, C1428EGA Ciudad de Buenos Aires, Argentina; email: saram@bg.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a 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. |l eng | |
| 593 | |a Departamento de Biodiversidad Y Biología Experimental, Facultad de Ciencias Exactas Y Naturales, Ciudad de Buenos Aires, Buenos Aires, Argentina | ||
| 593 | |a Instituto de Biotecnología, Centro de Investigación de Ciencias Veterinarias Y Agronómicas, Instituto Nacional de Tecnología Agropecuaria, Hurlingham, Buenos Aires, Argentina | ||
| 593 | |a Instituto de Recursos Biológicos, Centro de Investigación de Recursos Naturales, Instituto Nacional de Tecnología Agropecuaria, Hurlingham, Buenos Aires, Argentina | ||
| 593 | |a Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, C1428EGA Ciudad de Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a CHENOPODIUM QUINOA |
| 690 | 1 | 0 | |a DEHYDRIN |
| 690 | 1 | 0 | |a ENVIRONMENT |
| 690 | 1 | 0 | |a IN SITU IMMUNOLOCALIZATION |
| 690 | 1 | 0 | |a QUINOA CULTIVAR |
| 690 | 1 | 0 | |a WESTERN BLOT ANALYSIS |
| 690 | 1 | 0 | |a DEHYDRIN PROTEINS, PLANT |
| 690 | 1 | 0 | |a VEGETABLE PROTEIN |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CELL FRACTIONATION |
| 690 | 1 | 0 | |a CHENOPODIUM QUINOA |
| 690 | 1 | 0 | |a MERISTEM |
| 690 | 1 | 0 | |a METABOLISM |
| 690 | 1 | 0 | |a PLANT SEED |
| 690 | 1 | 0 | |a PRENATAL DEVELOPMENT |
| 690 | 1 | 0 | |a PROTEIN TRANSPORT |
| 690 | 1 | 0 | |a ULTRASTRUCTURE |
| 690 | 1 | 0 | |a WESTERN BLOTTING |
| 690 | 1 | 0 | |a BLOTTING, WESTERN |
| 690 | 1 | 0 | |a CHENOPODIUM QUINOA |
| 690 | 1 | 0 | |a MERISTEM |
| 690 | 1 | 0 | |a PLANT PROTEINS |
| 690 | 1 | 0 | |a PROTEIN TRANSPORT |
| 690 | 1 | 0 | |a SEEDS |
| 690 | 1 | 0 | |a SUBCELLULAR FRACTIONS |
| 690 | 1 | 0 | |a CHENOPODIUM QUINOA |
| 700 | 1 | |a Castellión, M. | |
| 700 | 1 | |a Distéfano, A.J. | |
| 700 | 1 | |a Del Vas, M. | |
| 700 | 1 | |a Maldonado, S. | |
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