Display Settings:

Format

Send to:

Choose Destination

    FEBS Lett. 1999 Feb 19;445(1):27-30.

    The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor.

    Cobine P, Wickramasinghe WA, Harrison MD, Weber T, Solioz M, Dameron CT.

    National Research Centre for Environmental Toxicology, University of Queensland, Coopers Plains, Australia.

    Expression of the cop operon which effects copper homeostasis in Enterococcus 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 delivering 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 quantitatively transferred from Cu(I)CopZ to Zn(II)CopY, with displacement of the zinc(II) and transfer of copper from a non-luminescent, exposed, binding site in CopZ to a luminescent, solvent shielded, binding site in CopY.

    PMID: 10069368 [PubMed - indexed for MEDLINE]

    Supplemental Content

    Click here to read