ArticleBiochemistry2012
Identification of natural and artificial DNA substrates for light-activated LOV-HTH transcription factor EL222.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
46 citing papers in PubMed, 82 citations in OpenAlex.
- The PucR-type activator IppR regulates 2-isopropylphenol hydroxylation in strainApplied and environmental microbiology · 2026Article
- Multi-level precise regulation of gene transcription in the yeast Saccharomyces cerevisiae based on light-sensitive CRISPR/Cas systems.Nucleic acids research · 2026Article
- Design principles for optogenetic-based targeted protein degradation.Synthetic and systems biotechnology · 2026Review
- Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026Article
- Mammalian synthetic gene circuits for biopharmaceutical development & manufacture.NPJ systems biology and applications · 2025Review
- 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
- Optogenetic control of pheromone gradients and mating behavior in budding yeast.Life science alliance · 2025Article
- Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222.Nucleic acids research · 2025Article
- Optogenetic Control of Phosphate-Responsive Genes Using Single-Component Fusion Proteins inACS synthetic biology · 2024Article
- Optogenetic control of phosphate-responsive genes using single component fusion proteins inbioRxiv : the preprint server for biology · 2024Article
- Opticool: Cutting-edge transgenic optical tools.PLoS genetics · 2024Review
- Construction and Characterization of Light-Responsive Transcriptional Systems.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The N-Terminal Region of the BcWCL1 Photoreceptor Is Necessary for Self-Dimerization and Transcriptional Activation upon Light Stimulation in Yeast.International journal of molecular sciences · 2023Article
- Multidimensional characterization of inducible promoters and a highly light-sensitive LOV-transcription factor.Nature communications · 2023Article
- Optogenetics for transcriptional programming and genetic engineering.Trends in genetics : TIG · 2022Review
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- A Single-Component Blue Light-Induced System Based on EL222 inInternational journal of molecular sciences · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Light-oxygen-voltage (LOV) domains serve as the photosensory modules for a wide range of plant and bacterial proteins, conferring blue light-dependent regulation to effector activities as diverse as enzymes and DNA binding. LOV domains can also be engineered into a variety of exogenous targets, allowing similar regulation for new protein-based reagents. Common to these proteins is the ability for LOV domains to reversibly form a photochemical adduct between an internal flavin chromophore and the surrounding protein, using this to trigger conformational changes that affect output activity. Using the Erythrobacter litoralis protein EL222 model system that links LOV regulation to a helix-turn-helix (HTH) DNA binding domain, we demonstrated that the LOV domain binds and inhibits the HTH domain in the dark, releasing these interactions upon illumination [Nash, A. I., et al. (2011) Proc. Natl. Acad. Sci. U.S.A. 108, 9449-9454]. Here we combine genomic and in vitro selection approaches to identify optimal DNA binding sites for EL222. Within the bacterial host, we observe binding at several genomic sites using a 12 bp sequence consensus that is also found by in vitro selection methods. Sequence-specific alterations in the DNA consensus reduce EL222 binding affinity in a manner consistent with the expected binding mode, a protein dimer binding to two repeats. Finally, we demonstrate the light-dependent activation of transcription of two genes adjacent to an EL222 binding site. Taken together, these results shed light on the native function of EL222 and provide useful reagents for further basic and applications research of this versatile protein.
Indexed as
Identifiers
What OpenQuestion holds
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.