Date of Graduation

1999

Document Type

Thesis

Degree Type

MS

Committee Chair

Jeffrey L. Price

Abstract

The gene double-time (dbt) is a molecular component of the circadian clock. It encodes a protein kinase that is likely to be involved in the phosphorylation and degradation of period protein (PER). Immunoblot analysis with an antibody produced for this thesis showed that double-time protein (DBT) levels do not undergo a detectable circadian oscillation, and that the levels of DBT are comparable in a short-period mutation (dbtS ) and wild-type flies. Immunocytochemical detection of PER in head sections of dbtS and wild-type flies demonstrated that PER enters photoreceptor nuclei later and disappears sooner in dbtS than in wild type flies. Unlike perL , dbtS was not defective in temperature compensation of circadian period. perL ;dbtS double mutant flies exhibited circadian periods shorter than those of wild-type flies, but had the same lack of temperature compensation. So the lack of temperature compensation is not a secondary consequence of the long period of perL flies.

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