This Article Full Text Full Text (PDF) Supplemental material Other Versions of this Article: JB.01846-07v1 190/14/4997    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Google Scholar Articles by Hochgräfe, F. Articles by Hecker, M. PubMed PubMed Citation Articles by Hochgräfe, F. Articles by Hecker, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 2008, p. 4997-5008, Vol. 190, No. 14
0021-9193/08/$08.00+0     doi:10.1128/JB.01846-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Nitric Oxide Stress Induces Different Responses but Mediates Comparable Protein Thiol Protection in Bacillus subtilis and Staphylococcus aureus ^,

Falko Hochgräfe,^1, Carmen Wolf,^1, Stephan Fuchs,¹ Manuel Liebeke,² Michael Lalk,² Susanne Engelmann,¹ and Michael Hecker^1*

Institute for Microbiology, Ernst-Moritz-Arndt University, Greifswald, Germany,¹ Institute for Pharmaceutical Biology, Ernst-Moritz-Arndt University, Greifswald, Germany²

Received 23 November 2007/ Accepted 30 April 2008

The nonpathogenic 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 a two-dimensional gel approach. Metabolic labeling of the proteins revealed major changes in the synthesis pattern of cytosolic proteins after the 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 nuclear magnetic resonance analyses indicating that NO causes a drastically higher increase in the formation of lactate and butanediol in S. aureus than in B. subtilis. Monitoring the intracellular protein thiol state, we observed no increase in reversible or irreversible protein thiol modifications after NO stress 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.

Published ahead of print on 16 May 2008.

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

F.H. and C.W. contributed equally to this study.

This article has been cited by other articles:

• Kohler, C., von Eiff, C., Liebeke, M., McNamara, P. J., Lalk, M., Proctor, R. A., Hecker, M., Engelmann, S. (2008). A Defect in Menadione Biosynthesis Induces Global Changes in Gene Expression in Staphylococcus aureus. J. Bacteriol. 190: 6351-6364 [Abstract] [Full Text]