Journal
PLANTA
Volume 240, Issue 1, Pages 91-101Publisher
SPRINGER
DOI: 10.1007/s00425-014-2067-5
Keywords
Copper transport; Ctr-like proteins; Functional complementation; Metal homeostasis; Vitis; VvCTr1
Categories
Funding
- European Union Funds (FEDER/COMPETE-Operational Competitiveness Program) - Portuguese Foundation for Science and Technology [FCOMP-01-0124-FEDER-022692, FCOMP-01-0124-FEDER-008760, FCT PTDC/AGR-ALI/100636/2008, FCT/5955/27/5/2013/S-scientific, SFRH/BD/64587/2009]
- networking activities within the European project INNOVINE [311775]
- European COST Action [FA1106]
- Will W. Lester Endowment University of California
- Fundação para a Ciência e a Tecnologia [SFRH/BD/64587/2009] Funding Source: FCT
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The Vitis vinifera copper transporter 1 is capable of self-interaction and mediates intracellular copper transport. An understanding of copper homeostasis in grapevine (Vitis vinifera L.) is particularly relevant to viticulture in which copper-based fungicides are intensively used. In the present study, the Vitis vinifera copper transporter 1 (VvCTr1), belonging to the Ctr family of copper transporters, was cloned and functionally characterized. Amino acid sequence analysis showed that VvCTr1 monomers are small peptides composed of 148 amino acids with 3 transmembrane domains and several amino acid residues typical of Ctr transporters. Bimolecular fluorescence complementation (BiFC) demonstrated that Ctr monomers are self-interacting and subcellular localization studies revealed that VvCTr1 is mobilized via the trans-Golgi network, through the pre-vacuolar compartment and located to the vacuolar membrane. The heterologous expression of VvCTr1 in a yeast strain lacking all Ctr transporters fully rescued the phenotype, while a deficient complementation was observed in a strain lacking only plasma membrane-bound Ctrs. Given the common subcellular localization of VvCTr1 and AtCOPT5 and the highest amino acid sequence similarity in comparison to the remaining AtCOPT proteins, Arabidopsis copt5 plants were stably transformed with VvCTr1. The impairment in root growth observed in copt5 seedlings in copper-deficient conditions was fully rescued by VvCTr1, further supporting its involvement in intracellular copper transport. Expression studies in V. vinifera showed that VvCTr1 is mostly expressed in the root system, but transcripts were also present in leaves and stems. The functional characterization of VvCTr-mediated copper transport provides the first step towards understanding the physiological and molecular responses of grapevines to copper-based fungicides.
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