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Science 4 June 2004:
Vol. 304. no. 5676, pp. 1503 - 1506
DOI: 10.1126/science.1096973
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Reports

Roles of the Two Drosophila CRYPTOCHROME Structural Domains in Circadian Photoreception

Ania Busza,1* Myai Emery-Le,1* Michael Rosbash,2 Patrick Emery1{dagger}

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 (crym) 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.

1 Department of Neurobiology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA.
2 Howard Hughes Medical Institute, Brandeis University, 415 South Street, Waltham, MA 02454, USA.



* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: patrick.emery{at}umassmed.edu

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