JB Accepts, published online ahead of print on 16 May 2008

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J. Bacteriol. doi:10.1128/JB.01846-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus

Falko Hochgräfe, Carmen Wolf, Stephan Fuchs, Manuel Liebeke, Michael Lalk, Susanne Engelmann, and Michael Hecker^*

Institute for Microbiology, Ernst-Moritz-Arndt University, Greifswald, Germany; Institute for Pharmaceutical Biology, Ernst-Moritz-Arndt University, Greifswald, Germany

^* To whom correspondence should be addressed. Email: hecker{at}uni-greifswald.de.

The non-pathogenic Bacillus subtilis and the pathogen Staphylococcus aureus are Gram-positive model organisms that have to cope with the radical nitric oxide (NO) generated by nitrite reductases of denitrifying bacteria and by the inducible NO synthases of immune cells of the host, respectively. The response of both microorganisms to NO was analyzed by using the two-dimensional gel approach. Metabolic labeling of the proteins revealed major changes in the synthesis pattern of cytosolic proteins after addition of the NO donor MAHMA NONOate. Whereas B. subtilis induced several oxidative stress responsive regulons controlled by Fur, PerR, OhrR, and Spx as well as the general stress response controlled by the alternative sigma factor SigB, the more resistant S. aureus showed an increased synthesis rate of proteins involved in anaerobic metabolism. These data were confirmed by NMR analyses indicating that NO causes a drastically higher increase in the formation of lactate and butanediol in S. aureus compared to B. subtilis. By monitoring the intracellular protein thiol state no increase in reversible or irreversible protein thiol modifications after NO stress was observed in either organism. Obviously, NO itself does not cause general protein thiol oxidations. In contrast, exposure of cells to NO prior to peroxide stress diminished the irreversible thiol oxidation caused by hydrogen peroxide.

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