double-time Is a Novel Drosophila Clock Gene that Regulates PERIOD Protein Accumulation

  title={double-time Is a Novel Drosophila Clock Gene that Regulates PERIOD Protein Accumulation},
  author={Jeffrey Price and Justin Blau and Adrian Rothenfluh and Marla Abodeely and Brian Kloss and Michael W. Young},

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The Drosophila double-timeS Mutation Delays the Nuclear Accumulation of period Protein and Affects the Feedback Regulation of period mRNA
Results suggest that dbt can regulate the feedback of per protein on its mRNA by delaying the time at which it is translocated to nuclei and altering the level of nuclear PER during the declining phase of the cycle.
A PER/TIM/DBT interval timer for Drosophila's circadian clock.
It is suggested that a cytoplasmic interval timer regulates nuclear translocation of PER/TIM/Doubletime (DBT) and TIM proteins, which are involved in the generation of circadian behavior in Drosophila.
A TIMELESS-Independent Function for PERIOD Proteins in the Drosophila Clock
Kinetics of Doubletime Kinase-dependent Degradation of the Drosophila Period Protein*
The study provides a simple model in which the changes in Drosophila behavioral rhythms can be explained solely by changes in the rate of PER degradation, which resembles that with wild-type DBT.
The Double-Time Protein Kinase Regulates the Subcellular Localization of the Drosophila Clock Protein Period
In this study, control of PER subcellular localization in Drosophila clock cells in vivo is examined and it is found that PER can translocate to the nucleus in tim01 null mutants but only if DBT kinase activity is inhibited, and nuclear PER is a potent transcriptional repressor in dbt mutants in vivo without TIM.
TIMELESS‐dependent positive and negative autoregulation in the Drosophila circadian clock
Analysis of period (per) mRNA levels and transcription uncovered a novel role for TIM in clock regulation: TIM increases per mRNA levels through a post‐transcriptional mechanism.
Drosophila doubletime Mutations Which either Shorten or Lengthen the Period of Circadian Rhythms Decrease the Protein Kinase Activity of Casein Kinase I
Low enzyme activity is associated with both short-period and long-period phenotypes of DBT in Drosophila melanogaster.


Block in nuclear localization of period protein by a second clock mutation, timeless.
The studies described here indicate that the nuclear localization of PER is blocked by timeless (tim), a second chromosome mutation that, like per null mutations, abolishes circadian rhythms.
Suppression of PERIOD protein abundance and circadian cycling by the Drosophila clock mutation timeless.
The tim mutant constitutively produces a low level of PER protein that is comparable with that produced late in the day by wild‐type flies and it is suggested that the multiple effects of tim are due to a primary effect on per expression at the posttranscriptional level.
Isolation of timeless by PER Protein Interaction: Defective Interaction Between timeless Protein and Long-Period Mutant PERL
The cloning of complementary DNAs derived from the tim gene in a two-hybrid screen for PER-interacting proteins and the demonstration of a physical interaction between the tim protein (TIM) and PER in vitro are reported.
A light-entrainment mechanism for the Drosophila circadian clock
The Per–Tim complex is a functional unit of the Drosophila circadian clock, and Tim degradation may be the initial response of the clock to light.