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The members of the cation diffusion facilitator (CDF) family transport heavy metal ions and play an important function in zinc ion homeostasis of the cell. A recent structure of an  Escherichia coli  CDF transporter protein YiiP has revealed its dimeric nature and autoregulatory zinc transport mechanism. Here, we report the cloning and heterologous production of four different CDF transporters, two each from the pathogenic mesophilic bacterium  Salmonella typhimurium  and from the hyperthermophilic bacterium  Aquifex aeolicus , in  E. coli  host cells. STM0758 of  S. typhimurium  was able to restore resistance to zinc ions when tested by complementation assays in the zinc-sensitive GG48 strain. Furthermore, copurification of bicistronically produced STM0758 and cross-linking experiments with the purified protein have revealed its possible oligomeric nature. The interaction between heavy metal ions and Aq_2073 of  A. aeolicus  was investigated by titration calorimetry. The entropy-driven, high-affinity binding of two Cd 2+  and two Zn 2+  per protein monomer with K d  values of around 100 n m  and 1 μ m , respectively, was observed. In addition, at least one more Zn 2+  can be bound per monomer with low affinity. This low-affinity site is likely to possess a functional role contributing to Zn 2+  transport across membranes.

biological chemistry

Heterologous production and functional and thermodynamic characterization of cation diffusion facilitator (CDF) transporters of mesophilic and hyperthermophilic origin