Abstract
The stressosome is a unique mediator of inducible gene expression in a wide variety of bacterial species. The 1.8 MDa stressosome complex in Bacillus subtilis is a key signal transducer in the environmental stress response of the bacterium, its activation leading ultimately to the upregulation of over 150 genes. The single particle cryo-EM derived molecular envelope of the stressosome was used to generate a pseudo-atomic model by fitting the crystal structures of known components of the complex. The final structure comprises three separate proteins, RsbR, RsbS and RsbT in an unusual arrangement with a pseudo-icosahedral core with sensory extensions provided by the N-terminal domain of RsbR. Immuno-localization studies of the stressosome in fixed B. subtilis cells showed that the complexes are located as punctate foci in the cytoplasm and are stable throughout the imposition of stress. Furthermore, we investigated the response to a number of environmental stressors and found that the response elicited by the stressosome showed a cooperative effect. Taken together, these results imply that the stressosome acts to integrate stress signals from multiple sources, and offers a tunable and co-operative response to activating signals. Our findings, as well as their implications for bacterial signaling, are further discussed in this addendum.