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Periplasmic metal-resistance protein CusF exhibits high affinity and specificity for both CuI and AgI.

Abstract：

:The periplasmic protein CusF, as a part of the CusCFBA efflux complex, plays a role in resistance to elevated levels of copper and silver in Escherichia coli. Although homologues have been identified in other Gram-negative bacteria, the substrate of CusF and its precise role in metal resistance have not been described. Here, isothermal titration calorimetry (ITC) was used to demonstrate that CusF binds with high affinity to both Cu(I) and Ag(I) but not Cu(II). The affinity of CusF for Ag(I) was higher than that for Cu(I), which could reflect more efficient detoxification of Ag(I) given the lack of a cellular need for Ag(I). The chemical shifts in the nuclear magnetic resonance (NMR) spectra of CusF-Ag(I) as compared to apo-CusF show that the region of CusF most affected by Ag(I) binding encompasses three absolutely conserved residues: H36, M47, and M49. This suggests that these residues may play a role in Ag(I) coordination. The NMR spectra of CusF in the presence of Cu(II) do not indicate specific binding, which is in agreement with the ITC data. We conclude that Cu(I) and Ag(I) are the likely physiological substrates.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Kittleson JT,Loftin IR,Hausrath AC,Engelhardt KP,Rensing C,McEvoy MM

doi

10.1021/bi0612622

subject

Has Abstract

pub_date

2006-09-19 00:00:00

pages

11096-102

issue

37

eissn

0006-2960

issn

1520-4995

journal_volume

45

pub_type

杂志文章

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