Skip Navigation


Molecular Plant Advance Access originally published online on June 7, 2007
Molecular Plant 2008 1(1):4-14; doi:10.1093/mp/ssm002
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
1/1/4    most recent
ssm002v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Rosenfeldt, G.
Right arrow Articles by Batschauer, A.
Right arrow Search for Related Content
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2007. Published by Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.

Chemically Induced and Light-Independent Cryptochrome Photoreceptor Activation

Gesa Rosenfeldta, Rafael Muñoz Vianaa, Henning D. Mootzb, Albrecht G. von Arnimc and Alfred Batschauera,1

a FB Biologie-Pflanzenphysiologie, Philipps-Universität, Karl-von-Frisch-Str. 8, 35032 Marburg, Germany
b Universität Dortmund, FB Chemie-Chemische Biologie, Otto-Hahn-Str. 6, 44227 Dortmund, Germany
c University of Tennessee, Department of Biochemistry, Cellular and Molecular Biology, Walters Life Sciences M407, Knoxville, TN 37996-0840, USA

1 To whom correspondence should be addressed. E-mail batschau{at}staff.uni-marburg.de, fax 49-(0)6421-282-1545.

The cryptochrome photoreceptors of higher plants are dimeric proteins. Their N-terminal photosensory domain mediates dimerization, and the unique C-terminal extension (CCT) mediates signaling. We made use of the human FK506-binding protein (FKBP) that binds with high affinity to rapamycin or rapamycin analogs (rapalogs). The FKBP–rapamycin complex is recognized by another protein, FRB, thus allowing rapamycin-induced dimerization of two target proteins. Here we demonstrate by bioluminescence resonance energy transfer (BRET) assays the applicability of this regulated dimerization system to plants. Furthermore, we show that fusion proteins consisting of the C-terminal domain of Arabidopsis cryptochrome 2 fused to FKBP and FRB and coexpressed in Arabidopsis cells specifically induce the expression of cryptochrome-controlled reporter and endogenous genes in darkness upon incubation with the rapalog. These results demonstrate that the activation of cryptochrome signal transduction can be chemically induced in a dose-dependent fashion and uncoupled from the light signal, and provide the groundwork for gain-of-function experiments to study specifically the role of photoreceptors in darkness or in signaling cross-talk even under light conditions that activate members of all photoreceptor families.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.