Browse the toolkit beneath workflows. The mechanism branch runs mechanism -> architecture -> component, while the technique branch runs from high-level approaches down to concrete methods.
15 items matching 1 filter
Mechanism Branch
Layer 1
Mechanisms
Top-level concepts: biophysical action modes such as heterodimerization, photocleavage, or RNA binding.
Layer 2
Architectures
Arrangements that realize or deploy mechanisms, including switches, construct patterns, and delivery strategies.
Layer 3
Components
Low-level parts and sequence-defined elements used inside architectures, including protein domains and RNA elements.
Technique Branch
Layer 1
Approaches
High-level engineering practices such as computational design, directed evolution, sequence verification, and functional assay.
Layer 2
Methods
Concrete methods used to design, build, verify, or characterize engineered systems.
Showing 1-15 of 15
OptoSTIM1 is an optogenetic protein tool engineered by combining the STIM1 SOAR region with a plant photoreceptor LOV2 domain. It manipulates intracellular Ca2+ levels by light-dependent activation of endogenous Ca2+-selective CRAC channels.
AcrIIC3-LOV2 is an engineered light-switchable anti-CRISPR protein formed by fusing the Neisseria meningitidis Cas9 inhibitor AcrIIC3 to the Avena sativa LOV2 blue-light sensory domain. In mammalian cells, two reported hybrids strongly inhibit NmeCas9 in the dark and allow robust genome editing under blue-light irradiation.
EL346 is a full-length blue light-activated histidine kinase from Erythrobacter litoralis HTCC2594 that contains a LOV photosensor domain. Structural evidence indicates that the LOV domain regulates kinase state by controlling intramolecular domain interactions, maintaining an inhibited dark-state conformation, and releasing that inhibition upon photoactivation.
The light-oxygen-voltage (LOV) sensor domain is a light-responsive regulatory protein domain characterized in the monomeric histidine kinase EL346. Structural evidence indicates that it binds one side of the DHpL domain to control kinase output, prevent dimerization, and release the catalytic apparatus from an inhibited conformation upon photoactivation.
LOV2 is a blue-light sensory domain from Avena sativa that was fused into the anti-CRISPR protein AcrIIC3 to create light-switchable inhibitors of Neisseria meningitidis Cas9. In this engineered context, AcrIIC3-LOV2 hybrids inhibited Nme Cas9 in the dark and permitted genome editing under blue light in mammalian cells.
The LOV2 domain from Avena sativa phototropin1 is a blue-light-responsive sensory domain that was fused to the restriction endonuclease PvuII to create a genetically encoded light-controllable chimeric nuclease. In this context, LOV2 modulates DNA cleavage activity in response to blue light, with the direction of regulation determined by the fusion interface.
A photosensitive domain-effector domain fusion is a construct design pattern in which a light-responsive protein domain is fused to an effector domain to generate light-controllable protein activity. The cited review presents this as a general engineering strategy for non-neuronal optogenetic proteins.
The catalytic/ATP-binding (CA) domain is the kinase catalytic module of the light-regulated histidine kinase EL346. In the reported structural model, its activity is regulated indirectly by LOV-domain photoactivation through changes in the DHpL/CA interface that release the CA domain from an inhibited dark-state conformation.
The A. sativa LOV2 domain is a light-responsive protein domain used as a regulatory module in engineered optogenetic switches. In a DHFR/LOV2 fusion, photoactivation thermally destabilized the fusion and lowered the catalytic transition free energy of the lit state relative to the dark state.
AsLOV2 REST-inhibitory chimeras are optogenetic fusion proteins that couple REST-inhibitory domains to the Avena sativa LOV2 photosensory module. In Neuro2a cells they enabled light-dependent modulation of REST target genes, and in primary neurons light-mediated REST inhibition increased Na+ currents and neuronal firing.
IDH-AsLOV2 is a photoswitchable isocitrate dehydrogenase created by inserting the AsLOV2 light-sensing domain into selected sites of IDH. In Escherichia coli, these engineered proteins were used to regulate tricarboxylic acid cycle flux and improve itaconic acid production under light control.
The LOV-PvuII fusion enzyme is a genetically encoded light-controllable endonuclease created by fusing the Avena sativa phototropin1 LOV2 photosensory domain to the restriction enzyme PvuII. In analyzed variants, blue light modulated DNA cleavage activity relative to dark conditions, with the direction of regulation determined by the fusion interface.
Light activated nuclear shuttle (LANS) is an optogenetic photoswitch built from the Avena sativa phototropin 1 LOV2 domain that drives light-dependent nuclear import of a fused target protein. It was engineered by embedding a nuclear import sequence into the LOV2 C-terminal helix to control nucleocytoplasmic distribution and associated transcription-related functions.
we developed an optogenetic tool named photoactivatable CaMKII (paCaMKII) by fusing a light-sensitive domain (LOV2) to CaMKIIα
TIP-LITer is a light-inducible TetR-based gene circuit component in which TetR is fused to a Tet-inhibitory peptide through the LOV2 photosensory domain. The reported design places inhibitory peptide control under light-sensitive regulation in mammalian cells.