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Lookup NU author(s): Sema Ejder,
Dr Jon Marles-WrightORCiD,
Professor Rick Lewis
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
The stressosome is a pseudo-icosahedral megadalton bacterial stress-sensing protein complex consisting of several copies of two STAS-domain proteins, RsbR and RsbS, and the kinase RsbT. Upon perception of environmental stress multiple copies of RsbT are released from the surface of the stressosome. Free RsbT activates downstream proteins to elicit a global cellular response, such as the activation of the general stress response in Gram-positive bacteria. The molecular events triggering RsbT release from the stressosome surface remain poorly understood. Here we present the map of Listeria innocua RsbR1/RsbS complex at resolutions of 3.45 Å for the STAS domain core in icosahedral symmetry and of 3.87 Å for the STAS domain and N-terminal sensors in D2 symmetry, respectively. The structure reveals a conformational change in the STAS domain linked to phosphorylation in RsbR. Docking studies indicate that allosteric RsbT binding to the conformationally flexible N-terminal sensor domain of RsbR affects the affinity of RsbS towards RsbT. Our results bring to focus the molecular events within the stressosome complex and further our understanding of this ubiquitous signaling hub.
Author(s): Miksys A, Fu L, Made MG, Guerreiro DN, Kaltwasser S, Conway M, Ejder S, Bruckmann A, Marles-Wright J, Lewis RJ, O'Byrne C, Pané-Farré J, Ziegler C
Publication type: Article
Publication status: Published
Journal: Communications Biology
Online publication date: 27/06/2022
Acceptance date: 31/05/2022
Date deposited: 23/11/2022
ISSN (electronic): 2399-3642
Publisher: Springer Nature
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