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Lookup NU author(s): Dr Olivier Delumeau
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In the pathway that controls σB activity, the RsbR-RsbS complex plays an important role by trapping RsbT, a positive regulator of σB of Bacillus subtilis. We have proposed that at the onset of stress, RsbR becomes phosphorylated, resulting in an enhanced activity of RsbT towards RsbS. RsbT is then free to interact with and activate RsbU, which in turn ultimately activates σB. In this study with purified proteins, we used mutant RsbR proteins to analyze the role of its phosphorylatable threonine residues. The results show that the phosphorylation of either of the two RsbT-phosphorylatable threonine residues (T171 and T205) in RsbR enhanced the kinase activity of RsbT towards RsbS. However, it appeared that RsbT preferentially phosphorylates T171. We also present in vitro evidence that identifies RsbX as a potential phosphatase for RsbR T205.
Author(s): Chen C-C, Yudkin MD, Delumeau O
Publication type: Article
Publication status: Published
Journal: Journal of Bacteriology
ISSN (print): 0021-9193
ISSN (electronic): 1067-8832
Publisher: American Society for Microbiology
PubMed id: 15466036
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