The grape aquaporin VvSIP1 transports water across the ER membrane
| Autor: | Olfa Zarrouk, Graça Soveral, François Chaumont, Henrique Noronha, Pierre Thiebaud, Hernâni Gerós, Alice Agasse, Ana Paula Martins, Dulceneia Gomes, Marie C. Berny, Serge Delrot |
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| Přispěvatelé: | Centro de Investigação e de Tecnologias Agro-Ambientais e Biológicas, Universidade do Minho, Universidade de Lisboa (ULISBOA), Université Catholique de Louvain = Catholic University of Louvain (UCL), Instituto Tecnologia Quimica e Biologica, Centre National de la Recherche Scientifique (CNRS), Ecophysiologie et Génomique Fonctionnelle de la Vigne (UMR EGFV), Institut National de la Recherche Agronomique (INRA)-Université Sciences et Technologies - Bordeaux 1-Université Victor Segalen - Bordeaux 2-Ecole Nationale Supérieure des Sciences Agronomiques de Bordeaux-Aquitaine (Bordeaux Sciences Agro) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
0106 biological sciences
Hot Temperature Physiology Xenopus [SDV]Life Sciences [q-bio] Gene Expression Aquaporin Saccharomyces cerevisiae Plant Science Biology Aquaporins Endoplasmic Reticulum 01 natural sciences Permeability 03 medical and health sciences chemistry.chemical_compound Gene Expression Regulation Plant Genes Reporter Tobacco Animals [SDV.BV]Life Sciences [q-bio]/Vegetal Biology Vitis Plant Proteins 030304 developmental biology Phosphatidylethanolamine 0303 health sciences Water transport Plant Stems Endoplasmic reticulum Vesicle Cell Membrane Major intrinsic proteins Water Biological Transport Biological membrane Up-Regulation Plant Leaves Membrane Biochemistry chemistry [SDE]Environmental Sciences Oocytes 010606 plant biology & botany |
| Zdroj: | Journal of Experimental Botany Journal of Experimental Botany, Oxford University Press (OUP), 2014, 65 (4), pp.981-993. ⟨10.1093/jxb/ert448⟩ |
| ISSN: | 0022-0957 1460-2431 |
| DOI: | 10.1093/jxb/ert448⟩ |
| Popis: | International audience; Water diffusion through biological membranes is facilitated by aquaporins, members of the widespread major intrinsic proteins (MIPs). In the present study, the localization, expression, and functional characterization of a small basic intrinsic protein (SIP) from the grapevine were assessed. VvSIP1 was expressed in leaves and berries from field-grown vines, and in leaves and stems from in vitro plantlets, but not in roots. When expressed in tobacco mesophyll cells and in Saccharomyces cerevisiae, fluorescent-tagged VvSIP1 was localized at the endoplasmic reticulum (ER). Stopped-flow spectroscopy showed that VvSIP1-enriched ER membrane vesicles from yeast exhibited higher water permeability and lower activation energy for water transport than control vesicles, indicating the involvement of protein-mediated water diffusion. This aquaporin was able to transport water but not glycerol, urea, sorbitol, glucose, or inositol. VvSIP1 expression in Xenopus oocytes failed to increase the water permeability of the plasma membrane. VvSIP1-His-tag was solubilized and purified to homogeneity from yeast ER membranes and the reconstitution of the purified protein in phosphatidylethanolamine liposomes confirmed its water channel activity. To provide further insights into gene function, the expression of VvSIP1 in mature grapes was studied when vines were cultivated in different field conditions, but its transcript levels did not increase significantly in water-stressed plants and western-exposed berries. However, the expression of the aquaporin genes VvSIP1, VvPIP2;2, and VvTIP1;1 was up-regulated by heat in cultured cells. |
| Databáze: | OpenAIRE |
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