The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation

Allison H. Williams (), Adam Redzej, Nathalie Rolhion, Tiago R. D. Costa, Aline Rifflet, Gabriel Waksman () and Pascale Cossart ()
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Allison H. Williams: Institut Pasteur, Groupe Avenir, INSERM
Adam Redzej: University College London and Birkbeck
Nathalie Rolhion: Institut Pasteur, Unité des Interactions Bactéries-Cellules
Tiago R. D. Costa: University College London and Birkbeck
Aline Rifflet: Institut Pasteur, Groupe Avenir, INSERM
Gabriel Waksman: University College London and Birkbeck
Pascale Cossart: Institut Pasteur, Unité des Interactions Bactéries-Cellules

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: Abstract How the stressosome, the epicenter of the stress response in bacteria, transmits stress signals from the environment has remained elusive. The stressosome consists of multiple copies of three proteins RsbR, RsbS and RsbT, a kinase that is important for its activation. Using cryo-electron microscopy, we determined the atomic organization of the Listeria monocytogenes stressosome at 3.38 Å resolution. RsbR and RsbS are organized in a 60-protomers truncated icosahedron. A key phosphorylation site on RsbR (T209) is partially hidden by an RsbR flexible loop, whose “open” or “closed” position could modulate stressosome activity. Interaction between three glutamic acids in the N-terminal domain of RsbR and the membrane-bound mini-protein Prli42 is essential for Listeria survival to stress. Together, our data provide the atomic model of the stressosome core and highlight a loop important for stressosome activation, paving the way towards elucidating the mechanism of signal transduction by the stressosome in bacteria.

Date: 2019
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DOI: 10.1038/s41467-019-10782-0

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