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

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

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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. © 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.


Publication metadata

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

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Letters

Year: 2003

Volume: 220

Issue: 1

Pages: 105-112

ISSN (print): 0378-1097

ISSN (electronic): 1574-6968

Publisher: Wiley-Blackwell

URL: http://dx.doi.org/10.1016/S0378-1097(03)00095-8

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

PubMed id: 12644235


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