ArticleBMC microbiology2015
Structure and function of a short LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae.
Article in BMC microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- Article
- Archaeal LOV domains from Lake Diamante: first functional characterization of a halo-adapted photoreceptor.Frontiers in microbiology · 2025Article
- Article
- LOV1 protein of Pseudomonas cichorii JBC1 modulates its virulence and lifestyles in response to blue light.Scientific reports · 2024Article
- Machine Learning-Assisted Engineering of Light, Oxygen, Voltage Photoreceptor Adduct Lifetime.JACS Au · 2023Article
- Origin and functional diversification of PAS domain, a ubiquitous intracellular sensor.Science advances · 2023Article
- Residue alterations within a conserved hydrophobic pocket influence light, oxygen, voltage photoreceptor dark recovery.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Class II LitR serves as an effector of "short" LOV-type blue-light photoreceptor in Pseudomonas mendocina.Scientific reports · 2022Article
- Regulation of the Erythrobacter litoralis DSM 8509 general stress response by visible light.Molecular microbiology · 2019Article
- Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein.PloS one · 2018Article
- Chemiosmotic Energy Conservation inFrontiers in microbiology · 2018Article
- Electron transfer pathways in a light, oxygen, voltage (LOV) protein devoid of the photoactive cysteine.Scientific reports · 2017Article
- Glutamine Amide Flip Elicits Long Distance Allosteric Responses in the LOV Protein Vivid.Journal of the American Chemical Society · 2017Article
- Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools.Scientific reports · 2017Article
- Photoactivation Reduces Side-Chain Dynamics of a LOV Photoreceptor.Biophysical journal · 2016Article
- Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations-implications for the understanding of LOV photoactivation.Frontiers in molecular biosciences · 2015Article
- Applications of hydrogen deuterium exchange (HDX) for the characterization of conformational dynamics in light-activated photoreceptors.Frontiers in molecular biosciences · 2015Review
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Authors and funding
14 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLight, oxygen, voltage (LOV) domains are widely distributed in plants, algae, fungi, bacteria, and represent the photo-responsive domains of various blue-light photoreceptor proteins. Their photocycle involves the blue-light triggered adduct formation between the C(4a) atom of a non-covalently bound flavin chromophore and the sulfur atom of a conserved cysteine in the LOV sensor domain. LOV proteins show considerable variation in the structure of N- and C-terminal elements which flank the LOV core domain, as well as in the lifetime of the adduct state.
resultsHere, we report the photochemical, structural and functional characterization of DsLOV, a LOV protein from the photoheterotrophic marine α-proteobacterium Dinoroseobacter shibae which exhibits an average adduct state lifetime of 9.6 s at 20°C, and thus represents the fastest reverting bacterial LOV protein reported so far. Mutational analysis in D. shibae revealed a unique role of DsLOV in controlling the induction of photopigment synthesis in the absence of blue-light. The dark state crystal structure of DsLOV determined at 1.5 Å resolution reveals a conserved core domain with an extended N-terminal cap. The dimer interface in the crystal structure forms a unique network of hydrogen bonds involving residues of the N-terminus and the β-scaffold of the core domain. The structure of photoexcited DsLOV suggests increased flexibility in the N-cap region and a significant shift in the Cα backbone of β strands in the N- and C-terminal ends of the LOV core domain.
conclusionsThe results presented here cover the characterization of the unusual short LOV protein DsLOV from Dinoroseobacter shibae including its regulatory function, extremely fast dark recovery and an N-terminus mediated dimer interface. Due to its unique photophysical, structural and regulatory properties, DsLOV might thus serve as an alternative model system for studying light perception by LOV proteins and physiological responses in bacteria.
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