An investigation of complex formation by the Drosophila circadian clock protein double-time and the effects of the double-time^S mutation on complex formation.

Author

• Madhavi Kalive, West Virginia University

Date of Graduation

1999

Document Type

Thesis

Degree Type

MS

College

Eberly College of Arts and Sciences

Department

Biology

Committee Chair

Jeffrey L. Price

Committee Member

Ashok Bidwai

Committee Member

Clifton Bishop

Abstract

The double-time ( dbt) gene in Drosophila encodes a protein (DBT) related to casein kinase I.This thesis examines whether DBT associates with other proteins besides PER, and whether the association of DBT might change as a function of time of day and genotype in vivo. DBT binds in vitro to several parts of PER and TIM, and to the N terminal of DBT. At all times of day in vivo, a significant fraction of DBT sediments with a molecular weight greater than that of its monomer. In dbtS flies, DBTS may associate more effectively than wild type DBT with other proteins. In timO and perO;timO mutant flies, DBT is complexed with other proteins, besides PER and TIM. An enhanced association between PER and DBTS proteins is predicted to alter the molecular oscillations of PER and TIM.

Recommended Citation

Kalive, Madhavi, "An investigation of complex formation by the Drosophila circadian clock protein double-time and the effects of the double-time^S mutation on complex formation." (1999). Graduate Theses, Dissertations, and Problem Reports. 10420.
https://researchrepository.wvu.edu/etd/10420