A marine cryptochrome with an inverse photo-oligomerization mechanism.

Autor: Vu HH; Institute of Molecular Physiology (IMP), Johannes Gutenberg-University Mainz, Hanns-Dieter-Hüsch-Weg 17, 55128, Mainz, Germany., Behrmann H; University of Cologne, Faculty of Mathematics and Natural Sciences, Institute of Biochemistry, Zülpicher Straße 47, 50674, Cologne, Germany., Hanić M; Institute of Physics, Carl von Ossietzky University of Oldenburg, Carl-von-Ossietzky Straße 9-11, 26129, Oldenburg, Germany., Jeyasankar G; University of Cologne, Faculty of Mathematics and Natural Sciences, Institute of Biochemistry, Zülpicher Straße 47, 50674, Cologne, Germany., Krishnan S; Institute of Molecular Physiology (IMP), Johannes Gutenberg-University Mainz, Hanns-Dieter-Hüsch-Weg 17, 55128, Mainz, Germany., Dannecker D; University of Cologne, Faculty of Mathematics and Natural Sciences, Institute of Biochemistry, Zülpicher Straße 47, 50674, Cologne, Germany., Hammer C; Institute of Molecular Physiology (IMP), Johannes Gutenberg-University Mainz, Hanns-Dieter-Hüsch-Weg 17, 55128, Mainz, Germany., Gunkel M; University of Cologne, Faculty of Mathematics and Natural Sciences, Institute of Biochemistry, Zülpicher Straße 47, 50674, Cologne, Germany., Solov'yov IA; Institute of Physics, Carl von Ossietzky University of Oldenburg, Carl-von-Ossietzky Straße 9-11, 26129, Oldenburg, Germany.; Research Center for Neurosensory Sciences, Carl von Ossietzky University of Oldenburg, Carl-von-Ossietzky Straße 9-11, 26111, Oldenburg, Germany.; Center for Nanoscale Dynamics (CENAD), Carl von Ossietzky Universität Oldenburg, Ammerländer Heerstr. 114-118, 26129, Oldenburg, Germany., Wolf E; Institute of Molecular Physiology (IMP), Johannes Gutenberg-University Mainz, Hanns-Dieter-Hüsch-Weg 17, 55128, Mainz, Germany. evawolf1@uni-mainz.de.; Institute of Molecular Biology (IMB), 55128, Mainz, Germany. evawolf1@uni-mainz.de., Behrmann E; University of Cologne, Faculty of Mathematics and Natural Sciences, Institute of Biochemistry, Zülpicher Straße 47, 50674, Cologne, Germany. elmar.behrmann@uni-koeln.de.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2023 Oct 30; Vol. 14 (1), pp. 6918. Date of Electronic Publication: 2023 Oct 30.
DOI: 10.1038/s41467-023-42708-2
Abstrakt: Cryptochromes (CRYs) are a structurally conserved but functionally diverse family of proteins that can confer unique sensory properties to organisms. In the marine bristle worm Platynereis dumerilii, its light receptive cryptochrome L-CRY (PdLCry) allows the animal to discriminate between sunlight and moonlight, an important requirement for synchronizing its lunar cycle-dependent mass spawning. Using cryo-electron microscopy, we show that in the dark, PdLCry adopts a dimer arrangement observed neither in plant nor insect CRYs. Intense illumination disassembles the dimer into monomers. Structural and functional data suggest a mechanistic coupling between the light-sensing flavin adenine dinucleotide chromophore, the dimer interface, and the C-terminal tail helix, with a likely involvement of the phosphate binding loop. Taken together, our work establishes PdLCry as a CRY protein with inverse photo-oligomerization with respect to plant CRYs, and provides molecular insights into how this protein might help discriminating the different light intensities associated with sunlight and moonlight.
(© 2023. The Author(s).)
Databáze: MEDLINE
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