Abstract
LOV domains act as biomolecular sensors for light, oxygen or the environment's redox potential. Conformational changes upon the formation of a covalent cysteinyl flavin adduct are propagated through hydrogen‐bonding networks in the core of designed hybrid phototropin LOV2 domains that incorporate the Bcl homology region 3 (BH3) of the key pro‐apoptotic protein BH3‐interacting‐domain death agonist (BID). The resulting change in conformation of a flanking amphiphilic α‐helix creates a light‐dependent optogenetic tool for the modulation of interactions with the anti‐apoptotic B‐cell leukaemia‐2 (Bcl‐2) family member Bcl‐xL.
Highlights
LOV domains act as biomolecular sensors for light, oxygen or the environment’s redox potential
LOV photosensors share a common mechanism by which a noncovalently bound flavin cofactor absorbs blue light (450–475 nm) to enter an excited electronic state; this leads to the formation of a covalent adduct between flavin mononucleotide (FMN) and the sulfur atom of a cysteine residue,[8] and significant conformational changes occur.[9]
Phototropin was one of the first blue-light receptors discovered in plants, and LOV2 from Avena sativa (AsLOV2) has previously been used for photoprotein engineering
Summary
LOV domains act as biomolecular sensors for light, oxygen or the environment’s redox potential. Sequence at residue 542 led to the widest dynamic His6-AsLOV2range between dark- and light-state affinities.
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