ArticleNature communications2019
The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Beyond Bactericidal: Plasma Surface Engineering to Defeat Food Matrix-Conditioning Layers.Comprehensive reviews in food science and food safety · 2026Review
- 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
- Cellular function of the GndA microprotein during heat shock.bioRxiv : the preprint server for biology · 2025Article
- Stress-dependent activation of themBio · 2025Article
- Phosphorylation State Dictates Bacterial Stressosome Assembly and Function.Research square · 2025Article
- Differential stress responsiveness determines intraspecies virulence heterogeneity and host adaptation in Listeria monocytogenes.Nature microbiology · 2024Article
- Large Roles of Small Proteins.Annual review of microbiology · 2024Review
- Ribosomal mutations enable a switch between high fitness and high stress resistance inFrontiers in microbiology · 2024Article
- Exposing the small protein load of bacterial life.FEMS microbiology reviews · 2023Review
- Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023Article
- Super-resolving microscopy reveals the localizations and movement dynamics of stressosome proteins in Listeria monocytogenes.Communications biology · 2023Article
- Article
- Molecular insights into intra-complex signal transmission during stressosome activation.Communications biology · 2022Article
- The Vibrio vulnificus stressosome is an oxygen-sensor involved in regulating iron metabolism.Communications biology · 2022Article
- Acid stress signals are integrated into the σB-dependent general stress response pathway via the stressosome in the food-borne pathogen Listeria monocytogenes.PLoS pathogens · 2022Article
- Listeria monocytogenes Requires the RsbX Protein To Prevent SigB Activation under Nonstressed Conditions.Journal of bacteriology · 2022Article
- Bacterial Small Membrane Proteins: the Swiss Army Knife of Regulators at the Lipid Bilayer.Journal of bacteriology · 2022Review
- Pathogenicity and virulence ofVirulence · 2021Article
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
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Authors and funding
7 authors.
Funding
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.
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