Michael J. Muskus

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A mutation (K38R) which specifically eliminates kinase activity was created in the Drosophila melanogaster ckI gene (doubletime [dbt]). In vitro, DBT protein carrying the K38R mutation (DBT(K/R)) interacted with Period protein (PER) but lacked kinase activity. In cell culture and in flies, DBT(K/R) antagonized the phosphorylation and degradation of PER, and(More)
Circadian rhythms are produced by a biological clock that is synchronized (or entrained) by cycles of light and temperature. In Drosophila, light triggers the interaction of the photoreceptor cryptochrome (CRY) with the circadian clock protein timeless (TIM). The absence of this interaction in cryb mutants eliminates this entrainment mechanism. The(More)
Mutations lowering the kinase activity of Drosophila Doubletime (DBT) and vertebrate casein kinase Iepsilon/delta (CKIepsilon/delta) produce long-period, short-period, and arrhythmic circadian rhythms. Since most ckI short-period mutants have been isolated in mammals, while the long-period mutants have been found mostly in Drosophila, lowered kinase(More)
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