Functional evolution of the photolyase/cryptochrome protein family: importance of the C terminus of mammalian CRY1 for circadian core oscillator performance.

@article{Chaves2006FunctionalEO,
  title={Functional evolution of the photolyase/cryptochrome protein family: importance of the C terminus of mammalian CRY1 for circadian core oscillator performance.},
  author={In{\^e}s Chaves and Kazuhiro Yagita and Sander Barnhoorn and Hitoshi Okamura and Gijsbertus T. J. van der Horst and Filippo Tamanini},
  journal={Molecular and cellular biology},
  year={2006},
  volume={26 5},
  pages={1743-53}
}
Cryptochromes (CRYs) are composed of a core domain with structural similarity to photolyase and a distinguishing C-terminal extension. While plant and fly CRYs act as circadian photoreceptors, using the C terminus for light signaling, mammalian CRY1 and CRY2 are integral components of the circadian oscillator. However, the function of their C terminus remains to be resolved. Here, we show that the C-terminal extension of mCRY1 harbors a nuclear localization signal and a putative coiled-coil… CONTINUE READING