Abstract
The cloning of double-time (dbt) is reported. DOUBLETIME protein (DBT) is most closely related to human casein kinase Iepsilon. dbtS and dbtL mutations, which alter period length of Drosophila circadian rhythms, produce single amino acid changes in conserved regions of the predicted kinase. dbtP mutants, which eliminate rhythms of per and tim expression and constitutively overproduce hypophosphorylated PER proteins, abolish most dbt expression. dbt mRNA appears to be expressed in the same cell types as are per and tim and shows no evident oscillation in wild-type heads. DBT is capable of binding to PER in vitro and in Drosophila cells, suggesting that a physical association of PER and DBT regulates PER phosphorylation and accumulation in vivo.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Biological Clocks / genetics*
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Casein Kinase 1 epsilon*
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Casein Kinases
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Conserved Sequence
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Drosophila / genetics*
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Drosophila Proteins*
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Gene Expression Regulation
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Genes, Insect*
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Genes, Lethal
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In Situ Hybridization
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Insect Proteins / metabolism
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Models, Biological
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Molecular Sequence Data
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Mutation
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Nuclear Proteins / metabolism
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Period Circadian Proteins
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Phosphorylation
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Protein Binding
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Protein Kinases / genetics*
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Sequence Homology, Amino Acid
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Time Factors
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Tissue Distribution
Substances
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Drosophila Proteins
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Insect Proteins
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Nuclear Proteins
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PER protein, Drosophila
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Period Circadian Proteins
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dco protein, Drosophila
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tim protein, Drosophila
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Protein Kinases
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Casein Kinase 1 epsilon
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Casein Kinases