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Molecular insights into intra-complex signal transmission during stressosome activation.

<div class='caption-title'>Cryo-EM derived reconstructions and models of the Listeria innocua stressosome complex (LiRsbRS) with imposed symmetry I2 to 3.45 Å (a–c) and in D2 to 3.87 Å (d, f) and fitted atomic models in the D2 map.</div>
<div class='caption-title'>Model of the STAS-domains in the stressosome complex from L. innocua.</div>
<div class='caption-title'>Phosphorylation sites and their surroundings in LiRsbRS.</div>
Miksys A, Fu L, Madej MG, Guerreiro DN, Kaltwasser S, Conway M, Ejder S, Bruckmann A, Marles-Wright J, Lewis RJ, O'Byrne C, Pané-Farré J, Ziegler C
OpenAccess logo Commun Biol 5 621 (2022)
Cited: 2 times
EuropePMC logo PMID: 35760945

Abstract

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.

Articles - 7b0u mentioned but not cited (1)

  1. Molecular insights into intra-complex signal transmission during stressosome activation. Miksys A, Fu L, Madej MG, Guerreiro DN, Kaltwasser S, Conway M, Ejder S, Bruckmann A, Marles-Wright J, Lewis RJ, O'Byrne C, Pané-Farré J, Ziegler C. Commun Biol 5 621 (2022)


Articles citing this publication (1)

  1. Computational and cellular exploration of the protein-protein interaction between Vibrio fischeri STAS domain protein SypA and serine kinase SypE. Milton ME, Visick KL. Commun Integr Biol 16 2203626 (2023)


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