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. 1991 Oct 15;88(20):8915–8919. doi: 10.1073/pnas.88.20.8915

Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins.

J S Cha 1, D A Cooksey 1
PMCID: PMC52621  PMID: 1924351

Abstract

Copper-resistant strains of Pseudomonas syringae pathovar tomato accumulate copper and develop blue colonies on copper-containing media. Three of the protein products of the copper-resistance operon (cop) were characterized to provide an understanding of the copper-resistance mechanism and its relationship to copper accumulation. The Cop proteins, CopA (72 kDa), CopB (39 kDa), and CopC (12 kDa), were produced only under copper induction. CopA and CopC were periplasmic proteins and CopB was an outer membrane protein. Leader peptide sequences of CopA, CopB, and CopC were confirmed by amino-terminal peptide sequencing. CopA, CopB, and CopC were purified from strain PT23.2, and their copper contents were determined. One molecule of CopA bound 10.9 +/- 1.2 atoms of copper and one molecule of CopC bound 0.6 +/- 0.1 atom of copper. The Cop proteins apparently mediate sequestration of copper outside of the cytoplasm as a copper-resistance mechanism.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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