ArticleBiochemistry2013
Blue light regulated two-component systems: enzymatic and functional analyses of light-oxygen-voltage (LOV)-histidine kinases and downstream response regulators.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Sequential structural changes in the monomeric LOV histidine kinase EL346 revealed by transient infrared spectroscopy.Physical chemistry chemical physics : PCCP · 2026Article
- Use of High Pressure NMR Spectroscopy to Rapidly Identify Proteins with Internal Ligand-Binding Voids.bioRxiv : the preprint server for biology · 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
- The blue light-dependent LOV-protein LdaP ofFrontiers in microbiology · 2024Article
- Article
- Tools to map target genes of bacterial two-component system response regulators.Environmental microbiology reports · 2020Review
- Regulation of the Erythrobacter litoralis DSM 8509 general stress response by visible light.Molecular microbiology · 2019Article
- Shining light on the alphaproteobacterial general stress response: Comment on: Fiebig et al., Mol Microbiol, 2019.Molecular microbiology · 2019Article
- Insights into histidine kinase activation mechanisms from the monomeric blue light sensor EL346.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Blue-Light Receptors for Optogenetics.Chemical reviews · 2018Review
- Allosteric control of a bacterial stress response system by an anti-σ factor.Molecular microbiology · 2018Article
- Structure and function of HWE/HisKA2-family sensor histidine kinases.Current opinion in microbiology · 2017Review
- Basis of Mutual Domain Inhibition in a Bacterial Response Regulator.Cell chemical biology · 2016Article
- Functional and topological diversity of LOV domain photoreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structured and Dynamic Disordered Domains Regulate the Activity of a Multifunctional Anti-σ Factor.mBio · 2015Article
- Ligand-induced folding of a two-component signaling receiver domain.Biochemistry · 2015Article
- LOV Histidine Kinase Modulates the General Stress Response System and Affects the virB Operon Expression in Brucella abortus.PloS one · 2015Article
- General Stress Signaling in the Alphaproteobacteria.Annual review of genetics · 2015Review
- Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Light is an essential environmental cue for diverse organisms. Many prokaryotic blue light photoreceptors use light, oxygen, voltage (LOV) sensory domains to control the activities of diverse output domains, including histidine kinases (HK). Upon activation, these proteins autophosphorylate a histidine residue before subsequently transferring the phosphate to an aspartate residue in the receiver domain of a cognate response regulator (RR). Such phosphorylation activates the output domain of the RR, leading to changes in gene expression, protein-protein interactions, or enzymatic activities. Here, we focus on one such light sensing LOV-HK from the marine bacterium Erythrobacter litoralis HTCC2594 (EL368), seeking to understand how kinase activity and subsequent downstream effects are regulated by light. We found that photoactivation of EL368 led to a significant enhancement in the incorporation of phosphate within the HK domain. Further enzymatic studies showed that the LOV domain affected both the LOV-HK turnover rate (kcat) and Km in a light-dependent manner. Using in vitro phosphotransfer profiling, we identified two target RRs for EL368 and two additional LOV-HKs (EL346 and EL362) encoded within the host genome. The two RRs include a PhyR-type transcriptional regulator (EL_PhyR) and a receiver-only protein (EL_LovR), reminiscent of stress-triggered systems in other bacteria. Taken together, our data provide a biochemical foundation for this light-regulated signaling module of sensors, effectors, and regulators that control bacterial responses to environmental conditions.
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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.