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

    Williams, A.H. and Redzej, Adam and Rolhion, N. and Costa, Tiago R.D. and Rifflet, A. and Waksman, Gabriel and Cossart, P. (2019) The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation. Nature Communications 10 (1), p. 3005. ISSN 2041-1723.

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    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    SWORD Depositor: Mr Joe Tenant
    Depositing User: Mr Joe Tenant
    Date Deposited: 25 Sep 2019 11:28
    Last Modified: 26 Sep 2019 14:50
    URI: http://eprints.bbk.ac.uk/id/eprint/28504

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