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. 2004 Jun 4;304(5676):1503-6.
doi: 10.1126/science.1096973.

Roles of the two Drosophila CRYPTOCHROME structural domains in circadian photoreception

Ania Busza  1 , Myai Emery-Le, Michael Rosbash, Patrick Emery
Affiliations

Roles of the two Drosophila CRYPTOCHROME structural domains in circadian photoreception

Ania Busza et al. Science. .

Abstract

CRYPTOCHROME (CRY) is the primary circadian photoreceptor in Drosophila. We show that CRY binding to TIMELESS (TIM) is light-dependent in flies and irreversibly commits TIM to proteasomal degradation. In contrast, CRY degradation is dependent on continuous light exposure, indicating that the CRY-TIM interaction is transient. A novel cry mutation (cry(m)) reveals that CRY's photolyase homology domain is sufficient for light detection and phototransduction, whereas the carboxyl-terminal domain regulates CRY stability, CRY-TIM interaction, and circadian photosensitivity. This contrasts with the function of Arabidopsis CRY domains and demonstrates that insect and plant cryptochromes use different mechanisms.

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