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      Characterization of the DNA- and metal-binding properties of Vibrio anguillarum fur reveals conservation of a structural Zn(2+) ion.

      Journal of Bacteriology
      Amino Acid Sequence, Bacterial Proteins, chemistry, genetics, metabolism, Cadmium, pharmacology, Cobalt, DNA, Bacterial, Escherichia coli, Genes, Bacterial, Manganese, Molecular Sequence Data, Nickel, Protein Binding, Repressor Proteins, Sequence Alignment, Vibrio, Zinc, analysis

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          Abstract

          The ferric uptake regulator, Fur, represses iron uptake and siderophore biosynthetic genes under iron-replete conditions. Here we report in vitro solution studies on Vibrio anguillarum Fur binding to the consensus 19-bp Escherichia coli iron box in the presence of several divalent metals. We found that V. anguillarum Fur binds the iron box in the presence of Mn(2+), Co(2+), Cd(2+), and to a lesser extent Ni(2+) but, unlike E. coli Fur, not in the presence of Zn(2+). We also found that V. anguillarum Fur contains a structural zinc ion that is necessary yet alone is insufficient for DNA binding.

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