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Publication : Roles of the two Drosophila CRYPTOCHROME structural domains in circadian photoreception.

First Author  Busza Ania Year  2004
Journal  Science Volume  304
Pages  1503-6 PubMed ID  15178801
Abstract Text  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. Doi  10.1126/science.1096973
Issue  5676 Month  Jun

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