A blue light receptor that mediates RNA binding and translational regulation.
Anna M WeberJennifer KaiserThea ZieglerSebastian PilslChristian RenzlLisa SixtGeorg PietruschkaSébastien MoniotAnkana KakotiMarc JuraschitzStefanie SchrottkeLaura LledóClemens SteegbornRobert BittlGünter MayerAndreas MöglichPublished in: Nature chemical biology (2019)
Sensory photoreceptor proteins underpin light-dependent adaptations in nature and enable the optogenetic control of organismal behavior and physiology. We identified the bacterial light-oxygen-voltage (LOV) photoreceptor PAL that sequence-specifically binds short RNA stem loops with around 20 nM affinity in blue light and weaker than 1 µM in darkness. A crystal structure rationalizes the unusual receptor architecture of PAL with C-terminal LOV photosensor and N-terminal effector units. The light-activated PAL-RNA interaction can be harnessed to regulate gene expression at the RNA level as a function of light in both bacteria and mammalian cells. The present results elucidate a new signal-transduction paradigm in LOV receptors and conjoin RNA biology with optogenetic regulation, thereby paving the way toward hitherto inaccessible optoribogenetic modalities.