Molecular Architecture of the "Stressosome," a Signal Integration and Transduction Hub

Author:

Marles-Wright Jon123,Grant Tim123,Delumeau Olivier123,van Duinen Gijs123,Firbank Susan J.123,Lewis Peter J.123,Murray James W.123,Newman Joseph A.123,Quin Maureen B.123,Race Paul R.123,Rohou Alexis123,Tichelaar Willem123,van Heel Marin123,Lewis Richard J.123

Affiliation:

1. Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle-upon-Tyne NE2 4HH, UK.

2. Faculty of Natural Sciences, Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK.

3. School of Environmental and Life Sciences, University of Newcastle, Collaghan, Newcastle, NSW 2308, Australia.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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