Abstract.
The ZAT1p zinc transporter from Arabidopsis thaliana (L.) Heynh. is a member of the cation diffusion facilitator (CDF) protein family. When heterologously expressed in Escherichia coli, ZAT1p bound zinc in a metal blot. Binding of zinc occurred mainly to the hydrophilic amino acid region from H182 to H232. A ZAT1p/ZAT1p*Δ(M1–I25) protein mixture was purified and reconstituted into proteoliposomes. Uptake of zinc into the proteoliposomes did not require a proton gradient across the liposomal membrane. ZAT1p did not transport cobalt, and transported cadmium at only 1% of the zinc transport rate. ZAT1p functioned as an uptake system for 65Zn2+ in two strains of the Gram-negative bacterium Ralstonia metallidurans, which were different in their content of zinc-efflux systems. The ZAT1 gene did not rescue increased zinc sensitivity of a ΔZRC1 single-mutant strain or of a ΔZRC1 ΔCOT1 double-mutant strain of Saccharomyces cerevisiae, but ZAT1 complemented this phenotype in a ΔSpZRC1 mutant strain of Schizosaccharomyces pombe.
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Bloß, T., Clemens, S. & Nies, D.H. Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana in microbial model organisms and reconstituted proteoliposomes. Planta 214, 783–791 (2002). https://doi.org/10.1007/s00425-001-0677-1
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DOI: https://doi.org/10.1007/s00425-001-0677-1