ArticleScientific reports2020
Impact of osmotic stress on the phosphorylation and subcellular location of Listeria monocytogenes stressosome proteins.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Downregulation of motility during stress requires stressosome input inApplied and environmental microbiology · 2026Article
- Stress-dependent activation of themBio · 2025Article
- Phosphorylation State Dictates Bacterial Stressosome Assembly and Function.Research square · 2025Article
- A single point mutation in theFrontiers in microbiology · 2024Article
- The Virulence and Infectivity of Listeria monocytogenes Are Not Substantially Altered by Elevated SigB Activity.Infection and immunity · 2023Article
- Stress Adaptation Responses of aFoods (Basel, Switzerland) · 2023Article
- Super-resolving microscopy reveals the localizations and movement dynamics of stressosome proteins in Listeria monocytogenes.Communications biology · 2023Article
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- Article
- Review
- 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
- The stressosome is required to transduce low pH signals leading to increased transcription of the amino acid-based acid tolerance mechanisms inAccess microbiology · 2022Article
- TheFrontiers in microbiology · 2022Article
- The Signal Peptide and Chaperone UNC93B1 Both Influence TLR8 Ectodomain Intracellular Endosomal Localization.Vaccines · 2021Article
- Pathogenicity and virulence ofVirulence · 2021Article
- Activation of the Listeria monocytogenes Stressosome in the Intracellular Eukaryotic Environment.Applied and environmental microbiology · 2021Article
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Authors and funding
5 authors.
Funding
Abstract
Listeria monocytogenes responds to environmental stress using a supra-macromolecular complex, the stressosome, to activate the stress sigma factor SigB. The stressosome structure, inferred from in vitro-assembled complexes, consists of the core proteins RsbR (here renamed RsbR1) and RsbS and, the kinase RsbT. The active complex is proposed to be tethered to the membrane and to support RsbR1/RsbS phosphorylation by RsbT and the subsequent release of RsbT following signal perception. Here, we show in actively-growing cells that L. monocytogenes RsbR1 and RsbS localize mostly in the cytosol in a fully phosphorylated state regardless of osmotic stress. RsbT however distributes between cytosolic and membrane-associated pools. The kinase activity of RsbT on RsbR1/RsbS and its requirement for maximal SigB activation in response to osmotic stress were demonstrated in vivo. Cytosolic RsbR1 interacts with RsbT, while this interaction diminishes at the membrane when RsbR1 paralogues (RsbR2, RsbR3 and RsbL) are present. Altogether, the data support a model in which phosphorylated RsbR1/RsbS may sustain basal SigB activity in unstressed cells, probably assuring a rapid increase in such activity in response to stress. Our findings also suggest that in vivo the active RsbR1-RsbS-RsbT complex forms only transiently and that membrane-associated RsbR1 paralogues could modulate its assembly.
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