ArticleCommunications biology2023
Super-resolving microscopy reveals the localizations and movement dynamics of stressosome proteins in Listeria monocytogenes.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- 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
- Super-Resolution Mapping and Quantification of Molecular Diffusion via Single-Molecule Displacement/Diffusivity Mapping (SMAccounts of chemical research · 2025Article
- Multiplex imaging analysis of the tumor immune microenvironment for guiding precision immunotherapy.Frontiers in immunology · 2025Review
- Large Roles of Small Proteins.Annual review of microbiology · 2024Review
- Dynamic structure of E. coli cytoplasm: supramolecular complexes and cell aging impact spatial distribution and mobility of proteins.Communications biology · 2024Article
- Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions.Chemical reviews · 2024Review
- Metabolic reprogramming in the food-borne pathogen Listeria monocytogenes as a critical defence against acid stress.FEMS microbiology letters · 2024Review
- Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023Article
- Simulation-based Reconstructed Diffusion unveils the effect of aging on protein diffusion in Escherichia coli.PLoS computational biology · 2023Article
- Physicochemical homeostasis in bacteria.FEMS microbiology reviews · 2023Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human pathogen Listeria monocytogenes can cope with severe environmental challenges, for which the high molecular weight stressosome complex acts as the sensing hub in a complicated signal transduction pathway. Here, we show the dynamics and functional roles of the stressosome protein RsbR1 and its paralogue, the blue-light receptor RsbL, using photo-activated localization microscopy combined with single-particle tracking and single-molecule displacement mapping and supported by physiological studies. In live cells, RsbR1 is present in multiple states: in protomers with RsbS, large clusters of stressosome complexes, and in connection with the plasma membrane via Prli42. RsbL diffuses freely in the cytoplasm but forms clusters upon exposure to light. The clustering of RsbL is independent of the presence of Prli42. Our work provides a comprehensive view of the spatial organization and intracellular dynamics of the stressosome proteins in L. monocytogenes, which paves the way towards uncovering the stress-sensing mechanism of this signal transduction pathway.
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