The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor
- 19 February 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 445 (1), 27-30
- https://doi.org/10.1016/s0014-5793(99)00091-5
Abstract
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.Keywords
This publication has 21 references indexed in Scilit:
- Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1Plant Physiology, 1998
- Identification and Functional Expression of HAH1, a Novel Human Gene Involved in Copper HomeostasisJournal of Biological Chemistry, 1997
- CopY Is a Copper-inducible Repressor of the Enterococcus hirae Copper ATPasesPublished by Elsevier ,1997
- The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury‐resistance proteinsMolecular Microbiology, 1995
- Copper and Silver Transport by CopB-ATPase in Membrane Vesicles of Enterococcus hiraeJournal of Biological Chemistry, 1995
- Distinct Regions of Cu(I)·ACE1 Contact Two Spatially Resolved DNA Major Groove SitesPublished by Elsevier ,1995
- Two trans-Acting Metalloregulatory Proteins Controlling Expression of the Copper-ATPases of Enterococcus hirae*Journal of Biological Chemistry, 1995
- Distinct metal binding configurations in ACE1Biochemistry, 1993
- [62] Luminescence spectroscopy of metallothioneinsMethods in Enzymology, 1991