Structure and Function of Animal Cryptochromes
- N. Öztürk*,
- S.-H. Song*,
- S. Özgür*,
- C. P. Selby*,
- L. Morrison*,
- C. Partch†,
- D. Zhong‡, and
- A. Sancar*
- *Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599
- †Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390
- ‡Departments of Physics, Chemistry, and Biochemistry, Programs of Biophysics, Chemical Physics, and Biochemistry, Ohio State University, Columbus, Ohio 43210
Abstract
Cryptochrome (CRY) is a photolyase-like flavoprotein with no DNA-repair activity but with known or presumed blue-light receptor function. Animal CRYs have DNA-binding and autokinase activities, and their flavin cofactor is reduced by photoinduced electron transfer. In Drosophila, CRY is a major circadian photoreceptor, and in mammals, the two CRY proteins are core components of the molecular clock and potential circadian photoreceptors. In mammals, CRYs participate in cell cycle regulation and the cellular response to DNA damage by controlling the expression of some cell cycle genes and by directly interacting with checkpoint proteins.
Footnotes
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