Identification of natural and artificial DNA substrates for light-activated LOV-HTH transcription factor EL222.

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

SUBMITTER: Rivera-Cancel G 

PROVIDER: S-EPMC3531242 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature