• Medientyp: E-Artikel
  • Titel: Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine
  • Beteiligte: Dietler, Julia; Gelfert, Renate; Kaiser, Jennifer; Borin, Veniamin; Renzl, Christian; Pilsl, Sebastian; Ranzani, Américo Tavares; García de Fuentes, Andrés; Gleichmann, Tobias; Diensthuber, Ralph P.; Weyand, Michael; Mayer, Günter; Schapiro, Igor; Möglich, Andreas
  • Erschienen: Springer Science and Business Media LLC, 2022
  • Erschienen in: Nature Communications, 13 (2022) 1
  • Sprache: Englisch
  • DOI: 10.1038/s41467-022-30252-4
  • ISSN: 2041-1723
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: AbstractIn 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.
  • Zugangsstatus: Freier Zugang