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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| Author(s) | | Borrelly GPM; Harwood CR; Radford DS; Robinson NJ; Cavet JS; Kihlken MA; Le Brun NE |
| Publication type | | Article |
| Journal | | FEMS Microbiology Letters |
| Year | | 2003 |
| Volume | | 220 |
| Issue | | 1 |
| Pages | | 105-112 |
| ISSN (print) | | 0168-6496 |
| ISSN (electronic) | | 1574-6941 |
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| Full text for this publication is not currently held within this repository. Alternative links are provided below where available. |
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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. |
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| Publisher | | Wiley-Blackwell Publishing Ltd. |
| URL | | http://dx.doi.org/10.1016/S0378-1097(03)00095-8 |
| DOI | | 10.1016/S0378-1097(03)00095-8 |
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