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CopZ Cu-metallochaperone from Bacillus subtilis interacts in vivo with Cu-induced Cu-exporter CopA, but enhances Cu atoms per cell

Lookup NU author(s): Dr David Radford, Dr Gilles Borrelly, Professor Colin Harwood, Professor Nigel Robinson, Dr Jennifer Cavet


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The structure of the hypothetical copper-metallochaperone CopZ from Bacillus subtilis and its predicted partner CopA have been studied but their respective contributions to copper export, -import, -sequestration and -supply are unknown. ΔcopA was hypersensitive to copper and contained more copper atoms cell−1 than wild-type. Expression from the copA operator-promoter increased in elevated copper (not other metals), consistent with a role in copper export. A bacterial two-hybrid assay revealed in vivo interaction between CopZ and the N-terminal domain of CopA but not that of a related transporter, YvgW, involved in cadmium-resistance. Activity of copper-requiring cytochrome caa3 oxidase was retained in ΔcopZ and ΔcopA. ΔcopZ was only slightly copper-hypersensitive but ΔcopZ/ΔcopA was more sensitive than ΔcopA, implying some action of CopZ that is independent of CopA. Significantly, ΔcopZ contained fewer copper atoms cell−1 than wild-type under these conditions. CopZ makes a net contribution to copper sequestration and/or recycling exceeding any donation to CopA for export.

Publication metadata

Author(s): Borrelly GPM; Harwood CR; Radford DS; Robinson NJ; Cavet JS; Kihlken MA; Le Brun NE

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Letters

Year: 2003

Volume: 220

Issue: 1

Pages: 105-112

ISSN (print): 0168-6496

ISSN (electronic): 1574-6941

Publisher: Wiley-Blackwell Publishing Ltd.


DOI: 10.1016/S0378-1097(03)00095-8


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