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Molecular and Cellular Biology, March 2006, p. 1743-1753, Vol. 26, No. 5
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.5.1743-1753.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Functional Evolution of the Photolyase/Cryptochrome Protein Family: Importance of the C Terminus of Mammalian CRY1 for Circadian Core Oscillator Performance{dagger}

Inês Chaves,1,{ddagger} Kazuhiro Yagita,2 Sander Barnhoorn,1 Hitoshi Okamura,3 Gijsbertus T. J. van der Horst,1* and Filippo Tamanini1,{ddagger}

MGC, Department of Cell Biology and Genetics, Erasmus University Medical Center, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands,1 Unit of Circadian Systems, Department of Biological Science, Nagoya University Graduate School of Science, Nagoya 464-8602, Japan,2 Division of Molecular Brain Science, Department of Brain Sciences, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan3

Received 16 August 2005/ Returned for modification 19 September 2005/ Accepted 13 December 2005

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 domain that drive nuclear localization via two independent mechanisms and shift the equilibrium of shuttling mammalian CRY1 (mCRY1)/mammalian PER2 (mPER2) complexes towards the nucleus. Importantly, deletion of the complete C terminus prevents mCRY1 from repressing CLOCK/BMAL1-mediated transcription, whereas a plant photolyase gains this key clock function upon fusion to the last 100 amino acids of the mCRY1 core and its C terminus. Thus, the acquirement of different (species-specific) C termini during evolution not only functionally separated cryptochromes from photolyase but also caused diversity within the cryptochrome family.

* Corresponding author. Mailing address: Department of Cell Biology and Genetics, Erasmus University Medical Center, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands. Phone: 31 10 4087455. Fax: 31 10 4089468. E-mail: g.vanderhorst{at}erasmusmc.nl.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} I.C. and F.T. contributed equally to this work.

Molecular and Cellular Biology, March 2006, p. 1743-1753, Vol. 26, No. 5
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.5.1743-1753.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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