Expression of the cop operon which effects copper homeostasis in Enterococc
us hirae is controlled by the copper responsive repressor CopY, Purified Zn
(II)CopY binds to a synthetic cop promoter fragment in vitro. Here we show
that the 8 kDa protein CopZ acts as a copper chaperone by specifically deli
vering copper(I) to Zn(II)CopY and releasing CopY from the DNA. As shown by
gel filtration and luminescence spectroscopy, two copper(I) are thereby qu
antitatively transferred from Cu(I)CopZ to Zn(II)CopY, with displacement of
the zinc(YI) and transfer of copper from a non-luminescent, exposed, bindi
ng site in CopZ to a luminescent, solvent shielded, binding site in CopY, (
C) 1999 Federation of European Biochemical Societies.