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Molecular architecture of the "stressosome," a signal integration and transduction hub

Lookup NU author(s): Dr Jon Marles-WrightORCiD, Dr Olivier Delumeau, Dr Susan Firbank, Dr James Murray, Dr Joseph Newman, Dr Maureen Quin, Professor Paul RaceORCiD, Professor Rick Lewis

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Abstract

A commonly used strategy by microorganisms to survive multiple stresses involves a signal transduction cascade that increases the expression of stress-responsive genes. Stress signals can be integrated by a multiprotein signaling hub that responds to various signals to effect a single outcome. We obtained a medium-resolution cryo-electron microscopy reconstruction of the 1.8-megadalton "stressosome" from Bacillus subtilis. Fitting known crystal structures of components into this reconstruction gave a pseudoatomic structure, which had a virus capsid-like core with sensory extensions. We suggest that the different sensory extensions respond to different signals, whereas the conserved domains in the core integrate the varied signals. The architecture of the stressosome provides the potential for cooperativity, suggesting that the response could be tuned dependent on the magnitude of chemophysical insult.

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Author(s): Marles-Wright J, Grant T, Delumeau O, van Duinen G, Firbank S, Lewis P, Murray J, Newman J, Quin M, Race P, Rohou A, Tichelaar W, van Heel M, Lewis RJ

Publication type: Article

Publication status: Published

Journal: Science

Year: 2008

Volume: 322

Issue: 5898

Pages: 92-96

ISSN (print): 0036-8075

ISSN (electronic): 1095-9203

Publisher: American Association for the Advancement of Science

URL: http://dx.doi.org/10.1126/science.1159572

DOI: 10.1126/science.1159572

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