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Journal of Bacteriology, April 2009, p. 2561-2573, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01514-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Role of RsbU in Controlling SigB Activity in Staphylococcus aureus following Alkaline Stress{triangledown}

Jan Pané-Farré,1 Beate Jonas,1,{dagger} Steven W. Hardwick,2,{ddagger} Katrin Gronau,1 Richard J. Lewis,2 Michael Hecker,1 and Susanne Engelmann1*

Institut für Mikrobiologie, Ernst-Moritz-Arndt-Universität, 17487 Greifswald, Germany,1 Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, United Kingdom2

Received 26 October 2008/ Accepted 28 January 2009

SigB is an alternative sigma factor that controls a large regulon in Staphylococcus aureus. Activation of SigB requires RsbU, a protein phosphatase 2C (PP2C)-type phosphatase. In a closely related organism, Bacillus subtilis, RsbU activity is stimulated upon interaction with RsbT, a kinase, which following an activating stimulus switches from a 25S high-molecular-weight complex, the stressosome, to the N-terminal domain of RsbU. Active RsbU dephosporylates RsbV and thereby triggers the release of SigB from its inhibitory complex with RsbW. While RsbU, RsbV, RsbW, and SigB are conserved in S. aureus, proteins similar to RsbT and the components of the stressosome are not, raising the question of how RsbU activity and hence SigB activity are controlled in S. aureus. We found that in contrast to the case in B. subtilis, the induced expression of RsbU was sufficient to stimulate SigB-dependent transcription in S. aureus. However, activation of SigB-dependent transcription following alkaline stress did not lead to a clear accumulation of SigB and its regulators RsbV and RsbW or to a change in the RsbV/RsbV-P ratio in S. aureus. When expressed in B. subtilis, the S. aureus RsbU displayed a high activity even in the absence of an inducing stimulus. This high activity could be transferred to the PP2C domain of the B. subtilis RsbU protein by a fusion to the N-terminal domain of the S. aureus RsbU. Collectively, the data suggest that the activity of the S. aureus RsbU and hence SigB may be subjected to different regulation in comparison to that in B. subtilis.

* Corresponding author. Mailing address: Institut für Mikrobiologie, Ernst-Moritz-Arndt-Universität, F.-L.-Jahn-Str. 15, D-17487 Greifswald, Germany. Phone: 49-3834-864227. Fax: 49-3834-864202. E-mail: Susanne.Engelmann{at}uni-greifswald.de

{triangledown} Published ahead of print on 6 February 2009.

{dagger} Present address: Institut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Schleswig-Holstein Campus Lübeck, 23538 Lübeck, Germany.

{ddagger} Present address: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, United Kingdom.

Journal of Bacteriology, April 2009, p. 2561-2573, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01514-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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