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

David S. Radford; Margaret A. Kihlken; Gilles P. M. Borrelly; Colin R. Harwood; Nick E. Le Brun; Jennifer S. Cavet

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

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

David S. Radford, Margaret A. Kihlken, Gilles P. M. Borrelly, Colin R. Harwood, Nick E. Le Brun, Jennifer S. Cavet

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	105-112
Number of pages	8
Journal	FEMS Microbiology Letters
Volume	220
Issue number	1
DOIs	https://doi.org/10.1016/S0378-1097(03)00095-8
Publication status	Published - 14 Mar 2003

Keywords

Atx1
CopA
CopZ
Cytochrome oxidase
Metallochaperone
P-type ATPase

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10.1016/S0378-1097(03)00095-8

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

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.",

keywords = "Atx1, CopA, CopZ, Cytochrome oxidase, Metallochaperone, P-type ATPase",

author = "Radford, {David S.} and Kihlken, {Margaret A.} and Borrelly, {Gilles P. M.} and Harwood, {Colin R.} and {Le Brun}, {Nick E.} and Cavet, {Jennifer S.}",

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T1 - CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA

AU - Radford, David S.

AU - Kihlken, Margaret A.

AU - Borrelly, Gilles P. M.

AU - Harwood, Colin R.

AU - Le Brun, Nick E.

AU - Cavet, Jennifer S.

PY - 2003/3/14

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N2 - 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.

AB - 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.

KW - Atx1

KW - CopA

KW - CopZ

KW - Cytochrome oxidase

KW - Metallochaperone

KW - P-type ATPase

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AN - SCOPUS:0347721765

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JO - FEMS Microbiology Letters

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ER -

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

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Keywords

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