ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 116 papers.
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Who cites it
116 citing papers in PubMed, 210 citations in OpenAlex.
- Sequential structural changes in the monomeric LOV histidine kinase EL346 revealed by transient infrared spectroscopy.Physical chemistry chemical physics : PCCP · 2026Article
- Illuminating cancer therapy: The translational path of optogenetics.Bioactive materials · 2026Review
- Multi-level precise regulation of gene transcription in the yeast Saccharomyces cerevisiae based on light-sensitive CRISPR/Cas systems.Nucleic acids research · 2026Article
- Article
- Design principles for optogenetic-based targeted protein degradation.Synthetic and systems biotechnology · 2026Review
- Small Molecule Regulation of CLOCK:BMAL1 DNA Binding Activity.bioRxiv : the preprint server for biology · 2026Article
- Magneto-Photonic Gene Circuit for Minimally Invasive Control of Gene Expression in Mammalian Cells.ACS omega · 2026Article
- Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026Article
- Magneto-Photonic Gene Circuit for Minimally Invasive Control of Gene Expression in Mammalian Cells.bioRxiv : the preprint server for biology · 2025Article
- MultiSite Assembly of Gateway Induced Clones (MAGIC): a flexible cloning toolbox for use in vertebrate model systems.Development (Cambridge, England) · 2025Article
- A pipeline for screening small molecule-enhanced protein stability in a bacterial orphan receptor.Protein science : a publication of the Protein Society · 2025Article
- A Pipeline for Screening Small Molecule-Enhanced Protein Stability in A Bacterial Orphan Receptor.bioRxiv : the preprint server for biology · 2025Article
- Potent optogenetic regulation of gene expression in mammalian cells for bioproduction and basic research.Nucleic acids research · 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
- Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222.Nucleic acids research · 2025Article
- Photochemistry of Receptor-Bound Flavin Resolved in Living Human Cells by Infrared Spectroscopy.Journal of the American Chemical Society · 2025Article
- Lighting up yeast: overview of optogenetics in yeast and their applications to yeast biotechnology.FEMS yeast research · 2025Review
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Optogenetic Control of Phosphate-Responsive Genes Using Single-Component Fusion Proteins inACS synthetic biology · 2024Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Light-oxygen-voltage (LOV) domains are blue light-activated signaling modules integral to a wide range of photosensory proteins. Upon illumination, LOV domains form internal protein-flavin adducts that generate conformational changes which control effector function. Here we advance our understanding of LOV regulation with structural, biophysical, and biochemical studies of EL222, a light-regulated DNA-binding protein. The dark-state crystal structure reveals interactions between the EL222 LOV and helix-turn-helix domains that we show inhibit DNA binding. Solution biophysical data indicate that illumination breaks these interactions, freeing the LOV and helix-turn-helix domains of each other. This conformational change has a key functional effect, allowing EL222 to bind DNA in a light-dependent manner. Our data reveal a conserved signaling mechanism among diverse LOV-containing proteins, where light-induced conformational changes trigger activation via a conserved interaction surface.
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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.