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

被引：79
作者：
Radford, DS
Kihlken, MA
Borrelly, GPM
Harwood, CR
Le Brun, NE
Cavet, JS [1 ]
机构：
[1] Newcastle Univ, Sch Med, Sch Cell & Mol Biosci, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England
[2] Univ E Anglia, Sch Chem Sci & Pharm, Norwich NR4 7TJ, Norfolk, England
来源：
FEMS MICROBIOLOGY LETTERS | 2003年 / 220卷 / 01期
基金：
英国生物技术与生命科学研究理事会;
关键词：
CopZ; CopA; metallochaperone; P-type ATPase; cytochrome oxidase; Atx1;
D O I：
10.1016/S0378-1097(03)00095-8
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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 -supple are unknovm. DeltacopA 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 A bacterial two-hybrid assay repealed in vivo interaction between CopZ and the N-terminal domain of CopA but not that of a related transporter, YvgW.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 caa(3) oxidase was retained in DeltacopZ and DeltacopA. DeltacopZ A,as only slightly copper-hypersensitive but DeltacopZ/DeltacopA was more sensitive than DeltacopA, implying some action of CopZ that is independent of CopA. Significantly, DeltacopZ 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. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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页码：105 / 112
页数：8
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