LOV Domain
A light oxygen voltage sensing region (LOV domain) is a protein sensor for sensing environmental conditions, which exists in various higher plants, microalgae, fungi and bacteria. The common feature of all LOV proteins is the blue light sensitive flavin chromophore, which is covalently connected to the protein core through adjacent cysteine residues in the signal state.
LOV domains have become one of the most commonly used optogenetic switches. Lov domain has been found to control gene expression through DNA binding and participate in redox dependent regulation. In recent years, LOV based optogenetic tools have become more and more popular in controlling numerous cellular events, including cell movement, subcellular organelle distribution, formation sites of membrane contact, microtubule dynamics, transcription, and protein degradation.
Creative BioMart provides plenty of services and related solutions based on the AsLOV2 switch system.
AsLOV2 Domain Switch System
Overview
The light control of functional peptides is a powerful tool for spatial and temporal control of cellular signal events. The photosensitive LOV2 domain encoded by Avena Sativa phototropin 1 (AsLOV2) gene can be used to reversibly regulate the affinity of peptides and their binding partners. Sequence analysis and molecular simulation were used to embed two peptides into the JA helix of the AsLOV2 domain while maintaining the AsLOV2 structure in the dark, but allowed in J α When the helix unfolds under light, it binds to effector proteins.
There are three AsLOV2-derived switches, iLID, LOVTRAP and TULIP
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Related solutions
Bidirectional expression system in filamentous fungus Trichoderma reesei.
AsLOV2 Controlled Cre Recombinase System
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| |
AsLOV2 |
iLID |
LOVTRAP |
TULIP |
| Photoreceptor |
AsLOV2 |
AsLOV2–SsrA |
AsLOV2 |
LOVpep (AsLOV2–ePDZpeptide) |
| Binding partner |
/ |
Stringent starvation protein B |
Zdark |
ePDZ |
| Cofactor |
FMN |
FMN |
FMN |
FMN |
| Source organism |
Avena Sativa |
Avena Sativa |
Avena Sativa |
Avena Sativa |
| Mode of action |
Intramolecular conformational change |
Heterodimerization |
Heterodimerization, dissociation |
Heterooligomerization |
| Excitation wavelength |
450 nm |
450 nm |
450 nm |
450 nm |
| Reversion wavelength |
Dark |
Dark |
Dark |
Dark |
| Excitation time |
Seconds |
Seconds |
Seconds |
Seconds |
| Reversion time |
Tens of seconds |
Seconds to minutes |
Seconds to minutes |
Seconds to minutes |
Light Inducible Dimer (iLID) Switch System
Overview
In the dark, the SsrA peptide is spatially prevented from binding to its natural binding partner SspB. When activated with blue light, the C-terminal helix of the LOV2 domain is separated from the protein to bind the SsrA peptide to SspB. Without optimization, the binding affinity of the switch to SspB changed doubly under light stimulation.
iLID changed its affinity for SspB by light stimulation more than 50 times. The crystal structure of ILID shows the key interaction between the LOV2 domain surface and phenylalanine, which is designed to more tightly fix the SRA peptide to the LOV2 domain in the dark.
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