| Structural highlights
Publication Abstract from PubMed
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 microM 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.
A blue light receptor that mediates RNA binding and translational regulation.,Weber AM, Kaiser J, Ziegler T, Pilsl S, Renzl C, Sixt L, Pietruschka G, Moniot S, Kakoti A, Juraschitz M, Schrottke S, Lledo Bryant L, Steegborn C, Bittl R, Mayer G, Moglich A Nat Chem Biol. 2019 Nov;15(11):1085-1092. doi: 10.1038/s41589-019-0346-y. Epub, 2019 Aug 26. PMID:31451761[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weber AM, Kaiser J, Ziegler T, Pilsl S, Renzl C, Sixt L, Pietruschka G, Moniot S, Kakoti A, Juraschitz M, Schrottke S, Lledo Bryant L, Steegborn C, Bittl R, Mayer G, Moglich A. A blue light receptor that mediates RNA binding and translational regulation. Nat Chem Biol. 2019 Nov;15(11):1085-1092. doi: 10.1038/s41589-019-0346-y. Epub, 2019 Aug 26. PMID:31451761 doi:http://dx.doi.org/10.1038/s41589-019-0346-y
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