Light-Dependent Sequestration of TIMELESS by CRYPTOCHROME

Most organisms have circadian clocks consisting of negative feedback loops of gene regulation that facilitate adaptation to cycles of light and darkness. In this study, CRYPTOCHROME (CRY), a protein involved in circadian photoperception in Drosophila, is shown to block the function of PERIOD/TIMELES...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1999-07, Vol.285 (5427), p.553-556
Main Authors: Ceriani, M. Fernanda, Darlington, Thomas K., Staknis, David, Más, Paloma, Petti, Allegra A., Weitz, Charles J., Kay, Steve A.
Format: Article
Language:English
Subjects:
Animals
Antibodies
Biological and medical sciences
Biological Clocks
Cell Line
Cell lines
Cell Nucleus - metabolism
Chromophores
Circadian Rhythm
Circadian rhythms
Classical genetics, quantitative genetics, hybrids
Cryptochromes
Cytoplasm - metabolism
Darkness
Dimerization
Drosophila
Drosophila Proteins
Embryonic cells
Eye Proteins
Feedback (Response)
Flavoproteins - genetics
Flavoproteins - metabolism
Fundamental and applied biological sciences. Psychology
Genetics of eukaryotes. Biological and molecular evolution
Green Fluorescent Proteins
Insect Proteins - genetics
Insect Proteins - metabolism
Insects
Invertebrata
Light
Luminescent Proteins
Mutation
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Period Circadian Proteins
Photoreceptor Cells, Invertebrate
Photoreceptors
Plasmids
Proteins
Receptors, G-Protein-Coupled
Recombinant Fusion Proteins - metabolism
Research Article
Sequestration (Chemistry)
Transfection
Treaties
Yeasts
Yeasts - genetics
Yeasts - metabolism
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Summary:Most organisms have circadian clocks consisting of negative feedback loops of gene regulation that facilitate adaptation to cycles of light and darkness. In this study, CRYPTOCHROME (CRY), a protein involved in circadian photoperception in Drosophila, is shown to block the function of PERIOD/TIMELESS (PER/TIM) heterodimeric complexes in a light-dependent fashion. TIM degradation does not occur under these conditions; thus, TIM degradation is uncoupled from abrogation of its function by light. CRY and TIM are part of the same complex and directly interact in yeast in a light-dependent fashion. PER/TIM and CRY influence the subcellular distribution of these protein complexes, which reside primarily in the nucleus after the perception of a light signal. Thus, CRY acts as a circadian photoreceptor by directly interacting with core components of the circadian clock.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.285.5427.553