Publication:

Role of RsbU in controlling SigB activity in Staphylococcus aureus following alkaline stress (2009)

Author(s): Pane-Farre J, Jonas B, Hardwick SW, Gronau K, Lewis RJ, Hecker M, Engelmann S

    Abstract: 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.

      • Date: 01-04-2009
      • Journal: Journal of Bacteriology
      • Volume: 191
      • Issue: 8
      • Pages: 2561-2573
      • Publisher: American Society for Microbiology
      • Publication type: Article
      • Bibliographic status: Published

      Keywords: Adaptation, Physiological

      Alkalies/*pharmacology

      Amino Acid Sequence

      Anti-Bacterial Agents/*pharmacology

      Bacterial Proteins/*biosynthesis

      Gene Expression Regulation, Bacterial

      Models, Biological

      Molecular Sequence Data

      Phosphoprotein Phosphatases/*metabolism

      Phosphoric Monoester Hydrolases/*metabolism

      Sigma Factor/*biosynthesis

      Staphylococcus aureus/*drug effects/*physiology

      Staff

      Professor Rick Lewis
      Prof of Structural Biology