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Journal of Bacteriology, November 2006, p. 7885-7892, Vol. 188, No. 22
0021-9193/06/$08.00+0     doi:10.1128/JB.00892-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

High-Molecular-Weight Complexes of RsbR and Paralogues in the Environmental Signaling Pathway of Bacillus subtilis{triangledown}

Olivier Delumeau,1,2,{dagger} Chien-Cheng Chen,1,{dagger},{ddagger} James W. Murray,2,§ Michael D. Yudkin,1 and Richard J. Lewis2*

Microbiology Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom,1 Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, University of Newcastle, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom2

Received 21 June 2006/ Accepted 30 August 2006

Bacillus subtilis has developed an intricate signal transduction cascade to respond to the imposition of a variety of stresses on the cell. Reversible protein phosphorylation and the formation of alternative protein-protein complexes modulate the activity of {sigma}B, the RNA polymerase sigma factor subunit responsible for the transcription of the general stress response genes. Some of the regulators of {sigma}B, such as RsbR and RsbS, are known to associate in a 25S complex, called the stressosome, that can bind RsbT until RsbT phosphorylates target residues in RsbR and RsbS. To date, the RsbR-RsbS complex appears to be the most upstream component of the {sigma}B regulatory pathway. This large structure is thought to play an important role in sensing and/or integrating signals from different physical stresses. The roles of the paralogues of RsbR that are found in B. subtilis remain unclear. We describe here how the RsbR paralogues copurify with RsbR from B. subtilis cell lysates, and we demonstrate in vitro that the paralogues form large complexes either with RsbS or with a prepurified RsbR-RsbS binary complex. We conclude from these biochemical studies that stressosomes in B. subtilis cells contain minimally RsbS and all of the RsbT-phosphorylatable RsbR paralogues.

* Corresponding author. Mailing address: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, United Kingdom. Phone: 44 191 222 5482. Fax: 44 191 222 7424. E-mail: r.lewis{at}ncl.ac.uk.

{triangledown} Published ahead of print on 8 September 2006.

{dagger} O.D. and C.C.-C. contributed equally to this study.

{ddagger} Present address: Department of Biotechnology, National Kaohsiung Normal University, No. 62, Shenjhong Rd., Yanchao Township, Kaohsiung County 82444, Taiwan.

§ Present address: Wolfson Laboratories, Department of Biological Sciences, Imperial College of London, London SW7 2AZ, United Kingdom.

Journal of Bacteriology, November 2006, p. 7885-7892, Vol. 188, No. 22
0021-9193/06/$08.00+0     doi:10.1128/JB.00892-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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