ArticlemBio2016
A Diguanylate Cyclase Acts as a Cell Division Inhibitor in a Two-Step Response to Reductive and Envelope Stresses.
Article in mBio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Transient inhibition of cell division in competent pneumococcal cells results from deceleration of the septal peptidoglycan complex.Nature communications · 2025Article
- Spatio-genetically coordinated TPR domain-containing proteins modulate c-di-GMP signaling in Vibrio vulnificus.PLoS pathogens · 2025Article
- Investigations on genomic, topological and structural properties of diguanylate cyclases involved inCurrent research in structural biology · 2025Article
- Genetic requirements for uropathogenicmSystems · 2024Article
- Article
- Innovative Strategies to Overcome Antimicrobial Resistance and Tolerance.Microorganisms · 2022Review
- Recent Advances in the Control of Clinically Important Biofilms.International journal of molecular sciences · 2022Review
- The Diguanylate Cyclase YfiN of Pseudomonas aeruginosa Regulates Biofilm Maintenance in Response to Peroxide.Journal of bacteriology · 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
- Shigella flexneri Diguanylate Cyclases Regulate Virulence.Journal of bacteriology · 2021Article
- Bacteriophage-mediated interference of the c-di-GMP signalling pathway in Pseudomonas aeruginosa.Microbial biotechnology · 2021Article
- Article
- Bacterial cell proliferation: from molecules to cells.FEMS microbiology reviews · 2021Review
- Article
- Article
- Under Elevated c-di-GMP in Escherichia coli, YcgR Alters Flagellar Motor Bias and Speed Sequentially, with Additional Negative Control of the Flagellar Regulon via the Adaptor Protein RssB.Journal of bacteriology · 2019Article
- Direct Interaction between the Two Z Ring Membrane Anchors FtsA and ZipA.Journal of bacteriology · 2019Article
- Differential Regulation of Genes for Cyclic-di-GMP Metabolism Orchestrates Adaptive Changes During Rhizosphere Colonization byFrontiers in microbiology · 2019Article
- Signaling specificity in the c-di-GMP-dependent network regulating antibiotic synthesis in Lysobacter.Nucleic acids research · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
unlabelledCell division arrest is a universal checkpoint in response to environmental assaults that generate cellular stress. In bacteria, the cyclic di-GMP (c-di-GMP) signaling network is one of several signal transduction systems that regulate key processes in response to extra-/intracellular stimuli. Here, we find that the diguanylate cyclase YfiN acts as a bifunctional protein that produces c-di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli YfiN localizes to the Z ring by interacting with early division proteins and stalls cell division by preventing the initiation of septal peptidoglycan synthesis. These studies reveal a new role for a diguanylate cyclase in responding to environmental change, as well as a novel mechanism for arresting cell division. IMPORTANCE: While the major role of c-di-GMP signaling is to control the decision to move freely or settle in a biofilm, recent studies show a broader range of output functions for c-di-GMP signaling. This work reports an unexpected second role for YfiN, a conserved diguanylate cyclase in Gram-negative bacteria, known to contribute to persistence in the host. We find that YfiN acts as a cell division inhibitor in response to envelope stress. Unlike known cell division inhibitors, the interaction of YfiN with cell division proteins retains the Z ring at the midcell but prevents septal invagination. The new function of YfiN not only emphasizes the versatility of c-di-GMP signaling but describes a novel mechanism for a cell division checkpoint.
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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.