期刊
SCIENCE
卷 304, 期 5676, 页码 1503-1506出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1096973
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资金
- NIGMS NIH HHS [GM66777-01, P01 GM33205] Funding Source: Medline
- NINDS NIH HHS [5 T32 NS07366-08, P01 NS44232] Funding Source: Medline
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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