ArticleProceedings of the National Academy of Sciences of the United States of America2022
Real-time detection of response regulator phosphorylation dynamics in live bacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Dynamic heterogeneity in an E. coli stress response regulon mediates gene activation and antimicrobial peptide tolerance.Cell reports · 2026Article
- Resisting the gallium "Trojan horse": Experimental evolutionary insights into microbial resistance.Gene & protein in disease · 2026Article
- Phosphorylation of a conserved intrinsically disordered region is necessary for activation of a bacterial Hanks-type Ser/Thr kinase signaling pathway.bioRxiv : the preprint server for biology · 2025Article
- Gradient matching accelerates mixed-effects inference for biochemical networks.Bioinformatics (Oxford, England) · 2025Article
- Gallium Resistance inApplied microbiology (Basel, Switzerland) · 2025Article
- Constitutive activation of two-component systems reveals regulatory network interactions in Streptococcus agalactiae.Nature communications · 2024Article
- Article
- Interplay between Two-Component Regulatory Systems Is Involved in Control of Cupriavidus metallidurans Metal Resistance Genes.Journal of bacteriology · 2023Article
- Real-time detection of response regulator phosphorylation dynamics in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Bacteria utilize two-component system (TCS) signal transduction pathways to sense and adapt to changing environments. In a typical TCS, a stimulus induces a sensor histidine kinase (SHK) to phosphorylate a response regulator (RR), which then dimerizes and activates a transcriptional response. Here, we demonstrate that oligomerization-dependent depolarization of excitation light by fused mNeonGreen fluorescent protein probes enables real-time monitoring of RR dimerization dynamics in live bacteria. Using inducible promoters to independently express SHKs and RRs, we detect RR dimerization within seconds of stimulus addition in several model pathways. We go on to combine experiments with mathematical modeling to reveal that TCS phosphosignaling accelerates with SHK expression but decelerates with RR expression and SHK phosphatase activity. We further observe pulsatile activation of the SHK NarX in response to addition and depletion of the extracellular electron acceptor nitrate when the corresponding TCS is expressed from both inducible systems and the native chromosomal operon. Finally, we combine our method with polarized light microscopy to enable single-cell measurements of RR dimerization under changing stimulus conditions. Direct in vivo characterization of RR oligomerization dynamics should enable insights into the regulation of bacterial physiology.
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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.