Me. Dembinska et al., CIRCADIAN CYCLING OF A PERIOD-BETA-GALACTOSIDASE FUSION PROTEIN IN DROSOPHILA - EVIDENCE FOR CYCLICAL DEGRADATION, Journal of biological rhythms, 12(2), 1997, pp. 157-172
The authors analyzed circadian features of two period-lacZ (peu-lacZ)
fusion genes in transgenic strains of Drosophila. Both genes manifest
circadian fluctuations of mRNA levels, but fluctuations of only the la
rger chimeric protein are apparent. Fusion protein cycling is indistin
guishable from the behavior of wild-type per protein (PER), including
apparent temporal regulation of phosphorylation state. Several argumen
ts indicate that the difference in the two constructs is proper regula
tion at the level of protein turnover: the smaller protein has much hi
gher levels; a P-galactosidase degradation product is visible in both
strains but fails to manifest cycling, presumably due to a long half-l
ife; and only the noncycling proteins accumulate as a function of adul
t age. The large cycling fusion protein also undergoes modest cycling
in an arrhythmic per(01) background. This is Light dependent, resemble
s the regulation of the timeless protein (TIM) by light, and reflects
a documented fusion protein-TIM interaction. The results are discussed
with respect to the posttranscriptional regulation that is necessary
for proper cycling of both PER and TIM as well as for clock function.