The alkynyl-functionalized photocleavable linker is a construct pattern used in caged antisense morpholino reagents, in which an ethynyl-bearing photocleavable linker is coupled to an oligonucleotide. In the caged state it inhibits DNA binding, and brief 405-nm illumination restores antisense activity through linker photocleavage.
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Mechanism Concept
DNA Binding
A protein binds DNA in a stimulus-dependent manner to regulate gene expression. Current coverage includes 2 architectures and 1 component. Representative components include AsLOV2-Jα.
3 total items2 architectures1 components
Architectures
LOV-TAP is an artificial light-activable allosteric protein constructed by ligating the AsLOV2-Jα photoswitch to the tryptophan repressor TrpR. It is designed to regulate protein-DNA association by coupling light-triggered changes in the LOV module to structural and electrostatic changes in the interdomain region that alter DNA binding.
Components
AsLOV2-Jα is the light-oxygen-voltage-2/Jα photoswitch domain from Avena sativa phototropin1. In the reported LOV-TAP fusion, ligation of AsLOV2-Jα to TrpR enables light-dependent control of DNA binding through photoinduced structural and electrostatic changes.