ArticleProceedings of the National Academy of Sciences of the United States of America2014
Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 101 citations in OpenAlex.
- Sequential structural changes in the monomeric LOV histidine kinase EL346 revealed by transient infrared spectroscopy.Physical chemistry chemical physics : PCCP · 2026Article
- An extension of jamdock-suite for virtual screening from raw chemical datasets.STAR protocols · 2026Article
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- An inhalable gallium-polyphenol nanoparticle blocks bacterial electron transport chain and signal transduction for anti-biofilm therapy.Bioactive materials · 2026Article
- Use of High Pressure NMR Spectroscopy to Rapidly Identify Proteins with Internal Ligand-Binding Voids.bioRxiv : the preprint server for biology · 2025Article
- An HWE-Family Histidine Kinase Modulates Brucella Cell Envelope Properties and Host Innate Immune Response.Molecular microbiology · 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
- Article
- Navigating the signaling landscape of Ralstonia solanacearum: a study of bacterial two-component systems.World journal of microbiology & biotechnology · 2024Review
- The blue light-dependent LOV-protein LdaP ofFrontiers in microbiology · 2024Article
- Origin and functional diversification of PAS domain, a ubiquitous intracellular sensor.Science advances · 2023Article
- Genetic Analysis Reveals a Requirement for the Hybrid Sensor Kinase RscS inJournal of bacteriology · 2023Article
- Gas and light: triggers of c-di-GMP-mediated regulation.FEMS microbiology reviews · 2023Review
- Blue light promotes zero-valent sulfur production in a deep-sea bacterium.The EMBO journal · 2023Article
- Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine.Nature communications · 2022Article
- Light-regulated gene expression in Bacteria: Fundamentals, advances, and perspectives.Frontiers in bioengineering and biotechnology · 2022Review
- Phylogenetic Analysis with Prediction of Cofactor or Ligand Binding for Pseudomonas aeruginosa PAS and Cache Domains.Microbiology spectrum · 2021Article
- Allosteric mechanism of signal transduction in the two-component system histidine kinase PhoQ.eLife · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Although histidine kinases (HKs) are critical sensors of external stimuli in prokaryotes, the mechanisms by which their sensor domains control enzymatic activity remain unclear. Here, we report the full-length structure of a blue light-activated HK from Erythrobacter litoralis HTCC2594 (EL346) and the results of biochemical and biophysical studies that explain how it is activated by light. Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer. Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain. The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark. Upon light stimulation, interdomain interactions weaken to facilitate activation. Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation. We suggest parallels between EL346 and dimeric HKs, with sensor-induced movements in the DHp similarly remodeling the DHp/CA interface as part of activation.
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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.