Journal
SCIENCE
Volume 311, Issue 5758, Pages 226-229Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1118126
Keywords
-
Categories
Funding
- NIGMS NIH HHS [GM54339] Funding Source: Medline
Ask authors/readers for more resources
In contrast to current models, fluorescence resonance energy transfer measurements using a single-cell imaging assay with fluorescent forms of PER and TIM showed that these proteins bind rapidly and persist in the cytoplasm while gradually accumulating in discrete foci. After similar to 6 hours, complexes abruptly dissociated, as PER and TIM independently moved to the nucleus in a narrow time frame. The per(L) mutation delayed nuclear accumulation in vivo and in our cultured cell system, but without affecting rates of PER/TIM assembly or dissociation. This finding points to a previously unrecognized form of temporal regulation that underlies the periodicity of the circadian clock.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available