A marine cryptochrome with an inverse photo-oligomerization mechanism.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
30 10 2023
30 10 2023
Historique:
received:
01
06
2023
accepted:
19
10
2023
medline:
1
11
2023
pubmed:
31
10
2023
entrez:
31
10
2023
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 37903809
doi: 10.1038/s41467-023-42708-2
pii: 10.1038/s41467-023-42708-2
pmc: PMC10616196
doi:
Substances chimiques
Cryptochromes
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6918Informations de copyright
© 2023. The Author(s).
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