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Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine

DOI zum Zitieren der Version auf EPub Bayreuth: https://doi.org/10.15495/EPub_UBT_00006654
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.

Further data

Item Type: Article in a journal
Keywords: Photobiology; Signal processing; X-ray crystallography; Mechanism of action
DDC Subjects: 500 Science > 570 Life sciences, biology
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Language: English
Originates at UBT: Yes
URN: urn:nbn:de:bvb:703-epub-6654-4
Date Deposited: 15 Sep 2022 09:51
Last Modified: 15 Sep 2022 09:51
URI: https://epub.uni-bayreuth.de/id/eprint/6654

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