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

Waksman, G; Redzej, A; Costa, T; (2019) The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation. Nature Communications , 10 , Article 3005. 10.1038/s41467-019-10782-0. Green open access

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Abstract

The stressosome is the epicenter of the stress response in bacteria, and one of the largest bacterial nanomachines. How the stressosome integrates and 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. Here using cryo-electron microscopy, we determined the atomic organization of the Listeria monocytogenes stressosome at 3.38Å resolution. The structure shows that RsbR and RsbS are organized in a 60 protomers truncated icosahedron. Two phosphorylation sites on RsbR (T175, T209) and one on RsbS (S56) are arranged on a horizontal row that is interrupted by a 13 amino acid flexible loop in RsbR. RsbR T175 and RsbS S56 are accessible on the surface and are phosphorylated under normal stress conditions. Access to T209 is partially hidden by the RsbR flexible loop, whose “open” or “closed” position, could modulate stressosome activation. Modification of the flexible loop or of residues involved in RsbR and RsbS interaction, results in a dominant negative phenotype. In addition, we showed that the 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. Taken together, our data provide the first atomic model of the stressosome core assembly, and highlight a loop that is important for stressosome activation, paving the way towards elucidating the structural basis of stressosome function in bacteria.

Type: Article
Title: The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation
Open access status: An open access version is available from UCL Discovery
DOI: 10.1038/s41467-019-10782-0
Publisher version: https://doi.org/10.1038/s41467-019-10782-0
Language: English
Additional information: © The Author(s) 2019. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/10076960
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