CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA.
FEMS Microbiol Lett
; 220(1): 105-12, 2003 Mar 14.
Article
em En
| MEDLINE
| ID: mdl-12644235
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. 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 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 caa(3) oxidase was retained in deltacopZ and deltacopA. DeltacopZ was 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.
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Bases de dados:
MEDLINE
Assunto principal:
Bacillus subtilis
/
Proteínas de Bactérias
/
Adenosina Trifosfatases
/
Chaperonas Moleculares
/
Cobre
/
Proteínas de Transporte de Cátions
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
FEMS Microbiol Lett
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Reino Unido