ArticleNPJ biofilms and microbiomes2022
GGDEF domain as spatial on-switch for a phosphodiesterase by interaction with landmark protein HubP.
Article in NPJ biofilms and microbiomes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 19 citations in OpenAlex.
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- Epigenetic cellular memory inProceedings of the National Academy of Sciences of the United States of America · 2025Article
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- A WYL domain transcription factor regulates Lactiplantibacillus plantarum intestinal colonization via perceiving c-di-GMP.Nature communications · 2025Article
- A deterministic, c-di-GMP-dependent program ensures the generation of phenotypically similar, symmetric daughter cells during cytokinesis.Nature communications · 2024Article
- Review
- Binding of GTP to BifA is required for the production of Pel-dependent biofilms inJournal of bacteriology · 2024Article
- The biofilm community resurfaces: new findings and post-pandemic progress.Journal of bacteriology · 2023Review
- Unveiling a Virulence-Regulating Mechanism in Aeromonas hydrophila: a Quantitative Exoproteomic Analysis of an AraC-Like Protein.Frontiers in immunology · 2023Article
- Polarity of c-di-GMP synthesis and degradation.microLife · 2023Review
- Recent advances and perspectives in nucleotide second messenger signaling in bacteria.microLife · 2023Review
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13 authors at 5 institutions in 1 country.
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Abstract
In bacteria, the monopolar localization of enzymes and protein complexes can result in a bimodal distribution of enzyme activity between the dividing cells and heterogeneity of cellular behaviors. In Shewanella putrefaciens, the multidomain hybrid diguanylate cyclase/phosphodiesterase PdeB, which degrades the secondary messenger c-di-GMP, is located at the flagellated cell pole. Here, we show that direct interaction between the inactive diguanylate cyclase (GGDEF) domain of PdeB and the FimV domain of the polar landmark protein HubP is crucial for full function of PdeB as a phosphodiesterase. Thus, the GGDEF domain serves as a spatially controlled on-switch that effectively restricts PdeBs activity to the flagellated cell pole. PdeB regulates abundance and activity of at least two crucial surface-interaction factors, the BpfA surface-adhesion protein and the MSHA type IV pilus. The heterogeneity in c-di-GMP concentrations, generated by differences in abundance and timing of polar appearance of PdeB, orchestrates the population behavior with respect to cell-surface interaction and environmental spreading.
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