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

FEMS Microbiol Lett. 2003 Mar 14;220(1):105-12. doi: 10.1016/S0378-1097(03)00095-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Motifs
  • Bacillus subtilis / drug effects
  • Bacillus subtilis / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Cation Transport Proteins / chemistry
  • Cation Transport Proteins / metabolism*
  • Copper / metabolism*
  • Copper / pharmacology
  • Drug Resistance, Bacterial / genetics
  • Enzyme Induction / drug effects
  • Gene Deletion
  • Gene Expression Regulation, Bacterial / drug effects
  • Ion Transport
  • Models, Biological
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism*
  • Mutagenesis
  • Protein Interaction Mapping
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Two-Hybrid System Techniques


  • Bacterial Proteins
  • Cation Transport Proteins
  • CopA protein, Bacteria
  • Molecular Chaperones
  • Recombinant Fusion Proteins
  • Copper
  • Adenosine Triphosphatases