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*Compound via MeSH
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*COPPER, ELEMENTAL
*GLUCOSE

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Journal of Bacteriology, October 2008, p. 6706-6717, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00450-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Adaptation of Aerobically Growing Pseudomonas aeruginosa to Copper Starvation{triangledown} ,{dagger}

Emanuela Frangipani,1 Vera I. Slaveykova,2 Cornelia Reimmann,1 and Dieter Haas1*

Département de Microbiologie Fondamentale, Université de Lausanne, CH-1015 Lausanne,1 Environmental Biophysical Chemistry, Ecole Polytechnique Fédérale, Station 2, CH-1015 Lausanne, Switzerland2

Received 2 April 2008/ Accepted 2 August 2008

Restricted bioavailability of copper in certain environments can interfere with cellular respiration because copper is an essential cofactor of most terminal oxidases. The global response of the metabolically versatile bacterium and opportunistic pathogen Pseudomonas aeruginosa to copper limitation was assessed under aerobic conditions. Expression of cioAB (encoding an alternative, copper-independent, cyanide-resistant ubiquinol oxidase) was upregulated, whereas numerous iron uptake functions (including the siderophores pyoverdine and pyochelin) were expressed at reduced levels, presumably reflecting a lower demand for iron by respiratory enzymes. Wild-type P. aeruginosa was able to grow aerobically in a defined glucose medium depleted of copper, whereas a cioAB mutant did not grow. Thus, P. aeruginosa relies on the CioAB enzyme to cope with severe copper deprivation. A quadruple cyo cco1 cco2 cox mutant, which was deleted for all known heme-copper terminal oxidases of P. aeruginosa, grew aerobically, albeit more slowly than did the wild type, indicating that the CioAB enzyme is capable of energy conservation. However, the expression of a cioA'-'lacZ fusion was less dependent on the copper status in the quadruple mutant than in the wild type, suggesting that copper availability might affect cioAB expression indirectly, via the function of the heme-copper oxidases.

* Corresponding author. Mailing address: Département de Microbiologie Fondamentale, Université de Lausanne, Bâtiment Biophore, CH-1015 Lausanne, Switzerland. Phone: 41 21 692 56 31. Fax: 41 21 692 56 35. E-mail: Dieter.Haas{at}unil.ch

{triangledown} Published ahead of print on 15 August 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, October 2008, p. 6706-6717, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00450-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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