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Lookup NU author(s): Dr Olivier Delumeau,
Dr James Murray,
Professor Rick Lewis
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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 σB, the RNA polymerase sigma factor subunit responsible for the transcription of the general stress response genes. Some of the regulators of σB, 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 σBregulatory 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. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Author(s): Delumeau O, Chen C, Murray J, Yudkin M, Lewis RJ
Publication type: Article
Publication status: Published
Journal: Journal of Bacteriology
ISSN (print): 0021-9193
ISSN (electronic): 1098-5530
Publisher: American Society for Microbiology
PubMed id: 16963570
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