A marine cryptochrome with an inverse photo-oligomerization mechanism

Hong Ha Vu, Heide Behrmann, Maja Hanić, Gayathri Jeyasankar, Shruthi Krishnan, Dennis Dannecker, Constantin Hammer, Monika Gunkel, Ilia A. Solov’yov, Eva Wolf () and Elmar Behrmann ()
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Hong Ha Vu: Johannes Gutenberg-University Mainz
Heide Behrmann: Institute of Biochemistry
Maja Hanić: Carl von Ossietzky University of Oldenburg
Gayathri Jeyasankar: Institute of Biochemistry
Shruthi Krishnan: Johannes Gutenberg-University Mainz
Dennis Dannecker: Institute of Biochemistry
Constantin Hammer: Johannes Gutenberg-University Mainz
Monika Gunkel: Institute of Biochemistry
Ilia A. Solov’yov: Carl von Ossietzky University of Oldenburg
Eva Wolf: Johannes Gutenberg-University Mainz
Elmar Behrmann: Institute of Biochemistry

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract 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.

Date: 2023
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DOI: 10.1038/s41467-023-42708-2

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