ArticleCommunications biology2022
Molecular insights into intra-complex signal transmission during stressosome activation.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 4 citations in OpenAlex.
- Downregulation of motility during stress requires stressosome input inApplied and environmental microbiology · 2026Article
- Translation control by altered start codon usage as a means of modulating the general stress response and virulence in Listeria monocytogenes.PLoS genetics · 2026Article
- Phosphorylation State Dictates Bacterial Stressosome Assembly and Function.Research square · 2025Article
- Stressosome-independent but RsbT-dependent environmental stress sensing in Bacillus subtilis.Nature communications · 2025Article
- Computational and cellular exploration of the protein-protein interaction betweenCommunicative & integrative biology · 2023Article
Corrections and comments
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Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
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