G. Multhaup et al., Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance, BIOC BIOP R, 288(1), 2001, pp. 172-177
Citations number
38
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Intracellular copper routing in Enterococcus hirae can be accomplished by t
he CopZ metallochaperone. Using surface plasmon resonance analysis, we show
here that CopZ interacts with the CopA copper ATPase. The binding affinity
of CopZ for CopA was increased in the presence of copper, due to a 15-fold
lower dissociation rate constant. Mutating the N-terminal copper binding m
otif of CopA from CxxC to SxxS abolished this copper-induced effect. Moreov
er, CopZ failed to show an interaction with an unrelated copper binding pro
tein used as a control. These results show that (i) the CopA copper ATPase
specifically interacts with the CopZ chaperone, (ii) this interaction is ba
sed on protein-protein interaction, and (iii) surface plasmon resonance is
a novel tool for quantitative analysis of metallochaperone-target interacti
ons. (C) 2001 Academic Press.