| Abstract
| - In this paper the interaction of cytoplasmic CopZ and the N-terminal domain of the CopAATPase from Bacillus subtilis has been studied by NMR through 15N−1H HSQC experiments in order tounderstand the role of the two proteins in the whole copper trafficking mechanism of the bacteria. Itappears that the two proteins interact in a fashion similar to that of the yeast homologue proteins [Arnesano,F., Banci, L., Bertini, I., Cantini, F., Ciofi-Baffoni, S., Huffman, D. L., and O'Halloran, T. V. (2001) J.Biol. Chem.276, 41365−41376], although the surface potentials are reversed. A structural model for theinteraction is proposed. 15N mobility studies on the free proteins and on their complex are also reported.From these data, it appears that copper is largely transferred from CopZ to CopA, thus suggesting theirpossible involvement in a detoxification process. Comparing functional data of homologous proteins ofother bacteria, it can be concluded that this class of proteins is involved in copper homeostasis but thespecific roles are species dependent.
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