ArticleBiochemistry2013
Light-induced subunit dissociation by a light-oxygen-voltage domain photoreceptor from Rhodobacter sphaeroides.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 81 citations in OpenAlex.
- Illuminating cancer therapy: The translational path of optogenetics.Bioactive materials · 2026Review
- Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222.Nucleic acids research · 2025Article
- Archaeal LOV domains from Lake Diamante: first functional characterization of a halo-adapted photoreceptor.Frontiers in microbiology · 2025Article
- Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- Design and Engineering of Light-Induced Base Editors Facilitating Genome Editing with Enhanced Fidelity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
- Current Trends of Bacterial and Fungal Optoproteins for Novel Optical Applications.International journal of molecular sciences · 2023Review
- LOV2-based photoactivatable CaMKII and its application to single synapses: Local Optogenetics.Biophysics and physicobiology · 2023Article
- Class II LitR serves as an effector of "short" LOV-type blue-light photoreceptor in Pseudomonas mendocina.Scientific reports · 2022Article
- Optogenetics for transcriptional programming and genetic engineering.Trends in genetics : TIG · 2022Review
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- 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
- Genetic Factors Affect the Survival and Behaviors of Selected Bacteria during Antimicrobial Blue Light Treatment.International journal of molecular sciences · 2021Review
- QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.Physical chemistry chemical physics : PCCP · 2021Article
- Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1.Scientific reports · 2021Article
- Visual pH Sensors: From a Chemical Perspective to New Bioengineered Materials.Molecules (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Light-oxygen-voltage (LOV) domains bind a flavin chromophore to serve as blue light sensors in a wide range of eukaryotic and prokaryotic proteins. LOV domains are associated with a variable effector domain or a separate protein signaling partner to execute a wide variety of functions that include regulation of kinases, generation of anti-sigma factor antagonists, and regulation of circadian clocks. Here we present the crystal structure, photocycle kinetics, association properties, and spectroscopic features of a full-length LOV domain protein from Rhodobacter sphaeroides (RsLOV). RsLOV exhibits N- and C-terminal helical extensions that form an unusual helical bundle at its dimer interface with some resemblance to the helical transducer of sensory rhodopsin II. The blue light-induced conformational changes of RsLOV revealed from a comparison of light- and dark-state crystal structures support a shared signaling mechanism of LOV domain proteins that originates with the light-induced formation of a flavin-cysteinyl photoadduct. Adduct formation disrupts hydrogen bonding in the active site and propagates structural changes through the LOV domain core to the N- and C-terminal extensions. Single-residue variants in the active site and dimer interface of RsLOV alter photoadduct lifetimes and induce structural changes that perturb the oligomeric state. Size exclusion chromatography, multiangle light scattering, small-angle X-ray scattering, and cross-linking studies indicate that RsLOV dimerizes in the dark but, upon light excitation, dissociates into monomers. This light-induced switch in oligomeric state may prove to be useful for engineering molecular associations in controlled cellular settings.
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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.