ArticleBiophysical journal2008
A blue light inducible two-component signal transduction system in the plant pathogen Pseudomonas syringae pv. tomato.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 54 citations in OpenAlex.
- LOV1 protein of Pseudomonas cichorii JBC1 modulates its virulence and lifestyles in response to blue light.Scientific reports · 2024Article
- Class II LitR serves as an effector of "short" LOV-type blue-light photoreceptor in Pseudomonas mendocina.Scientific reports · 2022Article
- Genetic Factors Affect the Survival and Behaviors of Selected Bacteria during Antimicrobial Blue Light Treatment.International journal of molecular sciences · 2021Review
- Article
- A light life together: photosensing in the plant microbiota.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Review
- Light Response ofJournal of bacteriology · 2020Article
- Ultraviolet Radiation From a Plant Perspective: The Plant-Microorganism Context.Frontiers in plant science · 2020Review
- Signal transduction schemes inComputational and structural biotechnology journal · 2020Review
- A Noncanonical Chromophore Reveals Structural Rearrangements of the Light-Oxygen-Voltage Domain upon Photoactivation.Biochemistry · 2019Article
- Structure and function of a short LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae.BMC microbiology · 2015Article
- Short LOV Proteins in Methylocystis Reveal Insight into LOV Domain Photocycle Mechanisms.PloS one · 2015Article
- LOV Histidine Kinase Modulates the General Stress Response System and Affects the virB Operon Expression in Brucella abortus.PloS one · 2015Article
- Blue light regulated two-component systems: enzymatic and functional analyses of light-oxygen-voltage (LOV)-histidine kinases and downstream response regulators.Biochemistry · 2013Article
- Article
- A LOV protein modulates the physiological attributes of Xanthomonas axonopodis pv. citri relevant for host plant colonization.PloS one · 2012Article
- Blue and red light modulates SigB-dependent gene transcription, swimming motility and invasiveness in Listeria monocytogenes.PloS one · 2011Article
- LOVely enzymes - towards engineering light-controllable biocatalysts.Microbial biotechnology · 2010Review
- A non-hydrolyzable ATP derivative generates a stable complex in a light-inducible two-component system.The Journal of biological chemistry · 2009Article
- Distribution and phylogeny of light-oxygen-voltage-blue-light-signaling proteins in the three kingdoms of life.Journal of bacteriology · 2009Article
- Mechanism-based tuning of a LOV domain photoreceptor.Nature chemical biology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The open reading frame PSPTO2896 from the plant pathogen Pseudomonas syringae pv. tomato encodes a protein of 534 amino acids showing all salient features of a blue light-driven two-component system. The N-terminal LOV (light, oxygen, voltage) domain, potentially binding a flavin chromophore, is followed by a histidine kinase (HK) motif and a response regulator (RR). The full-length protein (PST-LOV) and, separately, the RR and the LOV+HK part (PST-LOV(DeltaRR)) were heterologously expressed and functionally characterized. The two LOV proteins showed typical LOV-like spectra and photochemical reactions, with the blue light-driven, reversible formation of a covalent flavin-cysteine bond. The fluorescence changes in the lit state of full-length PST-LOV, but not in PST-LOV(DeltaRR), indicating a direct interaction between the LOV core and the RR module. Experiments performed with radioactive ATP uncover the light-driven kinase activity. For both PST-LOV and PST-LOV(DeltaRR), much more radioactivity is incorporated when the protein is in the lit state. Furthermore, addition of the RR domain to the fully phosphorylated PST-LOV(DeltaRR) leads to a very fast transfer of radioactivity, indicating a highly efficient HK activity and a tight interaction between PST-LOV(DeltaRR) and RR, possibly facilitated by the LOV core itself.
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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.