Characterization of a multicopper oxidase gene from Staphylococcus aureus.
A multicopper oxidase gene from Staphylococcus aureus was cloned and overexpressed. Purified recombinant multicopper oxidase oxidized the substrate 3,3'-dimethoxybenzidine in the presence of copper. Disruption of mco showed copper sensitivity and H(2)O(2) resistance, suggesting roles for mco in copper homeostasis and oxidative stress response. Northern blot analysis showed copper-induced mco transcription.
Sitthisak
S
S
Microbiology Group, Department of Biological Sciences, Illinois State University, Normal, IL 61790-4120, USA.
Howieson
K
K
Amezola
C
C
Jayaswal
R K
RK
D003001:Cloning, Molecular; D003300:Copper / Q000378:metabolism* / Q000494:pharmacology; D003962:Dianisidine / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D018869:Heat-Shock Response; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010088:Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D017422:Sequence Analysis, DNA; D013211:Staphylococcus aureus / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics / Q000502:physiology
D003300:Copper; D006861:Hydrogen Peroxide; D010088:Oxidoreductases; C024748:copper oxidase; D003962:Dianisidine