Journal
NATURE COMMUNICATIONS
Volume 13, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-022-30252-4
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [491183248, MO2192/6-1, MO2192/6-2, MO2192/8-1, MA3442/5-1, MA3442/5-2]
- Alexander-vonHumboldt Foundation (Sofja-Kovalevskaya Award)
- DFG [SFB 1078]
- Projekt DEAL
- University of Bayreuth
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This study investigates whether light-oxygen-voltage (LOV) photoreceptors can transduce light signals in the absence of a conserved glutamine residue. Results show that LOV photoreceptors can still generate effective signaling responses even without this key glutamine. Further structural analysis reveals highly similar light-induced conformational changes regardless of the presence of the glutamine. These findings have implications for biotechnological applications and suggest the evolutionary descent of LOV photoreceptors from redox-active flavoproteins.
Light-oxygen-voltage (LOV) photoreceptors perceive blue light to elicit spatio-temporally defined cellular responses, and their signalling process has been extensively characterized. Here the authors report that the light signal is still transduced in the absence of a conserved Gln residue, thought to be key. In nature as in biotechnology, light-oxygen-voltage photoreceptors perceive blue light to elicit spatiotemporally defined cellular responses. Photon absorption drives thioadduct formation between a conserved cysteine and the flavin chromophore. An equally conserved, proximal glutamine processes the resultant flavin protonation into downstream hydrogen-bond rearrangements. Here, we report that this glutamine, long deemed essential, is generally dispensable. In its absence, several light-oxygen-voltage receptors invariably retained productive, if often attenuated, signaling responses. Structures of a light-oxygen-voltage paradigm at around 1 angstrom resolution revealed highly similar light-induced conformational changes, irrespective of whether the glutamine is present. Naturally occurring, glutamine-deficient light-oxygen-voltage receptors likely serve as bona fide photoreceptors, as we showcase for a diguanylate cyclase. We propose that without the glutamine, water molecules transiently approach the chromophore and thus propagate flavin protonation downstream. Signaling without glutamine appears intrinsic to light-oxygen-voltage receptors, which pertains to biotechnological applications and suggests evolutionary descendance from redox-active flavoproteins.
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