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Molecular and Cellular Biology, March 2007, p. 2120-2129, Vol. 27, No. 6
0270-7306/07/$08.00+0     doi:10.1128/MCB.01638-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Structure/Function Analysis of Xenopus Cryptochromes 1 and 2 Reveals Differential Nuclear Localization Mechanisms and Functional Domains Important for Interaction with and Repression of CLOCK-BMAL1{triangledown}

Ellena A. van der Schalie, Francesca E. Conte, Karla E. Marz, and Carla B. Green*

Department of Biology, University of Virginia, Charlottesville, Virginia 22904

Received 1 September 2006/ Returned for modification 17 October 2006/ Accepted 20 December 2006

Circadian rhythms control the temporal arrangement of molecular, physiological, and behavioral processes within an organism and also synchronize these processes with the external environment. A cell autonomous molecular oscillator, consisting of interlocking transcriptional/translational feedback loops, drives the approximately 24-hour duration of these rhythms. The cryptochrome protein (CRY) plays a central part in the negative feedback loop of the molecular clock by translocating to the nucleus and repressing CLOCK and BMAL1, two transcription factors that comprise the positive elements in this cycle. In order to gain insight into the inner workings of this feedback loop, we investigated the structure/function relationships of Xenopus laevis CRY1 (xCRY1) and xCRY2 in cultured cells. The C-terminal tails of both xCRY1 and xCRY2 are sufficient for their nuclear localization but achieve it by different mechanisms. Through the generation and characterization of xCRY/photolyase chimeras, we found that the second half of the photolyase homology region (PHR) of CRY is important for repression through facilitating interaction with BMAL1. Characterization of these functional domains in CRYs will help us to better understand the mechanism of the known roles of CRYs and to elucidate new intricacies of the molecular clock.

* Corresponding author. Mailing address: 275 Gilmer Hall, Department of Biology, University of Virginia, P.O. Box 400328, Charlottesville, VA 22904-4328. Phone: (434) 982-5436. Fax: (434) 982-5626. E-mail: cbg8b{at}virginia.edu.

{triangledown} Published ahead of print on 8 January 2007.

Molecular and Cellular Biology, March 2007, p. 2120-2129, Vol. 27, No. 6
0270-7306/07/$08.00+0     doi:10.1128/MCB.01638-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • McCarthy, E. V., Baggs, J. E., Geskes, J. M., Hogenesch, J. B., Green, C. B. (2009). Generation of a Novel Allelic Series of Cryptochrome Mutants via Mutagenesis Reveals Residues Involved in Protein-Protein Interaction and CRY2-Specific Repression. Mol. Cell. Biol. 29: 5465-5476 [Abstract] [Full Text]  
  • Tamanini, F., Chaves, I., Bajek, M. I., van der Horst, G. T. J. (2007). Structure Function Analysis of Mammalian Cryptochromes. Cold Spring Harb Symp Quant Biol 72: 133-139 [Abstract]  


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