CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA

Radford, David S., Kihlken, Margaret A., Borrelly, Gilles P. M., Harwood, Colin R., Le Brun, Nick E. and Cavet, Jennifer S. (2003) CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA. FEMS Microbiology Letters, 220 (1). pp. 105-112. ISSN 0378-1097

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: atx1,copa,copz,cytochrome oxidase,metallochaperone,p-type atpase,microbiology,molecular biology,genetics ,/dk/atira/pure/subjectarea/asjc/2400/2404
Faculty \ School: Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups: Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Chemistry of Life Processes
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Depositing User: LivePure Connector
Date Deposited: 18 Jun 2025 09:30
Last Modified: 23 Jun 2025 10:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/99601
DOI: 10.1016/S0378-1097(03)00095-8

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