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The Bacterial Stressosome: A Modular System that Has Been Adapted to Control Secondary Messenger Signaling

Lookup NU author(s): Dr John Berrisford, Dr Arnaud Basle, Professor Rick Lewis, Dr Jon Marles-Wright

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Abstract

The stressosome complex regulates downstream effectors in response to environmental signals. In Bacillus subtilis, it activates the alternative sigma factor sigma(B), leading to the upregulation of the general stress regulon. Herein, we characterize a stressosome-regulated biochemical pathway in Moorella thermoacetica. We show that the presumed sensor, MtR, and the scaffold, MtS, form a pseudo-icosahedral structure like that observed in B. subtilis. The N-terminal domain of MtR is structurally homologous to B. subtilis RsbR, despite low sequence identity. The affinity of the switch kinase, MtT, for MtS decreases following MtS phosphorylation and not because of structural reorganization. Dephosphorylation of MtS by the PP2C type phosphatase MtX permits the switch kinase to rebind the stressosome to reset the response. We also show that MtT regulates cyclic di-GMP biosynthesis through inhibition of a GG(D/E)EF-type diguanylate cyclase, demonstrating that secondary messenger levels are regulated by the stressosome.


Publication metadata

Author(s): Quin MB, Berrisford JM, Newman JA, Baslé A, Lewis RJ, Marles-Wright J

Publication type: Article

Publication status: Published

Journal: Structure

Year: 2012

Volume: 20

Issue: 2

Pages: 350-363

Print publication date: 07/02/2012

Date deposited: 10/06/2013

ISSN (print): 0969-2126

ISSN (electronic): 1878-4186

Publisher: Cell Press

URL: http://dx.doi.org/10.1016/j.str.2012.01.003

DOI: 10.1016/j.str.2012.01.003


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