CopZ Cu-metallochaperone from Bacillus subtilis interacts in vivo with Cu-induced Cu-exporter CopA, but enhances Cu atoms per cell

  1. Lookup NU author(s)
  2. Dr David Radford
  3. Dr Gilles Borrelly
  4. Professor Colin Harwood
  5. Professor Nigel Robinson
  6. Dr Jennifer Cavet
Author(s)Borrelly GPM; Harwood CR; Radford DS; Robinson NJ; Cavet JS; Kihlken MA; Le Brun NE
Publication type Article
JournalFEMS Microbiology Letters
ISSN (print)0168-6496
ISSN (electronic)1574-6941
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
PublisherWiley-Blackwell Publishing Ltd.
Actions    Link to this publication

Altmetrics provided by Altmetric