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Abstract:
Cryptochromes (CRY) are photolyase-like blue-light receptorsthat mediate light responses in plants and animals. How plantcryptochromes act in response to blue light is not well understood.We report here the identification and characterization of theArabidopsis CIB1 (cryptochrome-interacting basic-helix-loop-helix)protein. CIB1 interacts with CRY2 (cryptochrome 2) in a bluelight–specific manner in yeast and Arabidopsis cells,and it acts together with additional CIB1-related proteins topromote CRY2-dependent floral initiation. CIB1 binds to G box(CACGTG) in vitro with a higher affinity than its interactionwith other E-box elements (CANNTG). However, CIB1 stimulatesFT messenger RNA expression, and it interacts with chromatinDNA of the FT gene that possesses various E-box elements exceptG box. We propose that the blue light–dependent interactionof cryptochrome(s) with CIB1 and CIB1-related proteins representsan early photoreceptor signaling mechanism in plants.
Department of Molecular, Cell, and Developmental Biology, University of California, Los Angeles, CA 90095, USA.
* To whom correspondence should be sent. E-mail: clin{at}mcdb.ucla.edu
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Pamela J. Hines (9 December 2008) Sci. Signal.1 (49), ec426.
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