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URN to cite this document: urn:nbn:de:bvb:703-epub-6654-4
Title data
Dietler, Julia ; Gelfert, Renate ; Kaiser, Jennifer ; Borin, Veniamin ; Renzl, Christian ; Pilsl, Sebastian ; Ranzani, Américo Tavares ; García de Funtes, Andrés ; Gleichmann, Tobias ; Diensthuber, Ralph P. ; Weyand, Michael ; Mayer, Günter ; Schapiro, Igor ; Möglich, Andreas:
Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine.
In: Nature Communications.
Vol. 13
(2022)
Issue 1
.
- No. 2618.
ISSN 2041-1723
DOI der Verlagsversion: https://doi.org/10.1038/s41467-022-30252-4
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Abstract
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 Å 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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