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The Journal of Neuroscience, October 15, 2000, 20(20):7547-7555
Two Novel doubletime Mutants Alter Circadian
Properties and Eliminate the Delay between RNA and Protein in
Drosophila
Vipin
Suri1,
Jeffery C.
Hall2, 4, and
Michael
Rosbash2, 3, 4
Graduate Departments of 1 Biochemistry and
2 Biology, 3 Howard Hughes Medical Institute,
and 4 National Science Foundation Center for Biological
Timing, Brandeis University, Waltham, Massachusetts 02454
Phosphorylation is an important feature of pacemaker organization
in Drosophila. Genetic and biochemical evidence suggests involvement of the casein kinase I homolog doubletime
(dbt) in the Drosophila circadian
pacemaker. We have characterized two novel dbt mutants.
Both cause a lengthening of behavioral period and profoundly alter
period (per) and
timeless (tim) transcript and protein
profiles. The PER profile shows a major difference from the wild-type
program only during the morning hours, consistent with a prominent role
for DBT during the PER monomer degradation phase. The transcript
profiles are delayed, but there is little effect on the protein
accumulation profiles, resulting in the elimination of the
characteristic lag between the mRNA and protein profiles. These results
and others indicate that light and post-transcriptional regulation play
major roles in defining the temporal properties of the protein curves
and suggest that this lag is unnecessary for the feedback regulation of
per and tim protein on per
and tim transcription.
Key words:
circadian; entrainment, Drosophila; CKI ; PERIOD; phosphorylation
Copyright © 2000 Society for Neuroscience 0270-6474/00/20207547-09$05.00/0
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