ArticlePLoS genetics2020
c-di-GMP inhibits LonA-dependent proteolysis of TfoY in Vibrio cholerae.
Article in PLoS genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Regulation of dgcZ in EPEC E2348/69 and the effect of partially deleting its CZB domain on the type III secretion system.FEMS microbiology letters · 2026Article
- Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dynamic Executors of Bacterial Signals: Functional Versatility and Regulatory Networks of c-di-GMP Effectors.Biomolecules · 2025Review
- Parallel regulatory circuits orchestrate biofilm formation in response to c-di-GMP levels and growth phase.PLoS genetics · 2025Article
- Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis.Microbial cell factories · 2024Article
- Cyclic Diguanylate in the Wild: Roles During Plant and Animal Colonization.Annual review of microbiology · 2024Review
- Structural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Regulation of type VI secretion systems at the transcriptional, posttranscriptional and posttranslational level.Microbiology (Reading, England) · 2023Review
- Evolution of cyclic di-GMP signalling on a short and long term time scale.Microbiology (Reading, England) · 2023Article
- Sporadic type VI secretion in seventh pandemicMicrobiology (Reading, England) · 2023Article
- Type VI Secretion Systems: Environmental and Intra-host Competition of Vibrio cholerae.Advances in experimental medicine and biology · 2023Article
- A complete twelve-gene deletion null mutant reveals that cyclic di-GMP is a global regulator of phase-transition and host colonization in Erwinia amylovora.PLoS pathogens · 2022Article
- Evolution of amBio · 2022Article
- The RNA-Binding Protein ProQ Impacts Exopolysaccharide Biosynthesis and Second Messenger Cyclic di-GMP Signaling in the Fire Blight Pathogen Erwinia amylovora.Applied and environmental microbiology · 2022Article
- Yin and Yang of Biofilm Formation and Cyclic di-GMP Signaling of the Gastrointestinal Pathogen Salmonella enterica Serovar Typhimurium.Journal of innate immunity · 2022Review
- Article
- The Vibrio cholerae Type Six Secretion System Is Dispensable for Colonization but Affects Pathogenesis and the Structure of Zebrafish Intestinal Microbiome.Infection and immunity · 2021Article
- Virulence Regulation and Innate Host Response in the Pathogenicity ofFrontiers in cellular and infection microbiology · 2020Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The LonA (or Lon) protease is a central post-translational regulator in diverse bacterial species. In Vibrio cholerae, LonA regulates a broad range of behaviors including cell division, biofilm formation, flagellar motility, c-di-GMP levels, the type VI secretion system (T6SS), virulence gene expression, and host colonization. Despite LonA's role in cellular processes critical for V. cholerae's aquatic and infectious life cycles, relatively few LonA substrates have been identified. LonA protease substrates were therefore identified through comparison of the proteomes of wild-type and ΔlonA strains following translational inhibition. The most significantly enriched LonA-dependent protein was TfoY, a known regulator of motility and the T6SS in V. cholerae. Experiments showed that TfoY was required for LonA-mediated repression of motility and T6SS-dependent killing. In addition, TfoY was stabilized under high c-di-GMP conditions and biochemical analysis determined direct binding of c-di-GMP to LonA results in inhibition of its protease activity. The work presented here adds to the list of LonA substrates, identifies LonA as a c-di-GMP receptor, demonstrates that c-di-GMP regulates LonA activity and TfoY protein stability, and helps elucidate the mechanisms by which LonA controls important V. cholerae behaviors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.