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.
MeSH Terms
Amino Acid Sequence
Bacterial Outer Membrane Proteins/biosynthesis,genetics
Bacterial Proteins/analysis,biosynthesis,genetics
Cation Transport Proteins
Copper/metabolism,pharmacology
Drug Resistance, Microbial/genetics
Immunoblotting
Molecular Sequence Data
Molecular Weight
Operon
Protein Sorting Signals/genetics
Pseudomonas/drug effects,genetics
Recombinant Fusion Proteins/analysis
Chemicals
Bacterial Outer Membrane Proteins
Bacterial Proteins
Cation Transport Proteins
CopA protein, Bacteria
CopC protein, Bacteria
Protein Sorting Signals
Recombinant Fusion Proteins
Copper
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cha J S
Department of Plant Pathology, University of California, Riverside 92521-0122.
Cooksey D A
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