ArticleNature communications2024
Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Review
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- A novel two-component system regulates shikimate pathway for thermal adaptation in Thermus thermophilus.Nucleic acids research · 2026Article
- Spectroscopic Analyses of Photoconversion in Phytochromes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Detection of Histidine Kinase Activities of Bacteriophytochromes with Phos-tag™ Acrylamide Gel Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Engineering NIR-sighted bacteria.eLife · 2025Article
- Untangling the Complexity of Two-Component Signal Transduction in Bacteria.Microorganisms · 2025Review
- Traits of Bathy Phytochromes and Application to Bacterial Optogenetics.ACS synthetic biology · 2025Article
- A Designed ZnJournal of the American Chemical Society · 2025Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.The Journal of biological chemistry · 2025Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.bioRxiv : the preprint server for biology · 2025Article
- Induction of bacterial expression at the mRNA level by light.Nucleic acids research · 2024Article
- Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.Nature communications · 2024Article
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Authors and funding
5 authors.
Funding
Abstract
Bacteria must constantly probe their environment for rapid adaptation, a crucial need most frequently served by two-component systems (TCS). As one component, sensor histidine kinases (SHK) control the phosphorylation of the second component, the response regulator (RR). Downstream responses hinge on RR phosphorylation and can be highly stringent, acute, and sensitive because SHKs commonly exert both kinase and phosphatase activity. With a bacteriophytochrome TCS as a paradigm, we here interrogate how this catalytic duality underlies signal responses. Derivative systems exhibit tenfold higher red-light sensitivity, owing to an altered kinase-phosphatase balance. Modifications of the linker intervening the SHK sensor and catalytic entities likewise tilt this balance and provide TCSs with inverted output that increases under red light. These TCSs expand synthetic biology and showcase how deliberate perturbations of the kinase-phosphatase duality unlock altered signal-response regimes. Arguably, these aspects equally pertain to the engineering and the natural evolution of TCSs.
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