@Article{IPB-2139,
author = {Bloß, T. and Clemens, S. and Nies, D. H.},
title = {{Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana in microbial model organisms and reconstituted proteoliposomes}},
year = {2002},
pages = {783-791},
journal = {Planta},
doi = {10.1007/s00425-001-0677-1},
volume = {214},
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.}    
}