HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 20, 14916-14922, May 18, 2007

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 282/20/14916    most recent M700616200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Banerjee, R. Articles by Batschauer, A. Search for Related Content PubMed PubMed Citation Articles by Banerjee, R. Articles by Batschauer, A. Social Bookmarking                      What's this?

The Signaling State of Arabidopsis Cryptochrome 2 Contains Flavin Semiquinone^*

Roopa Banerjee, Erik Schleicher, Stefan Meier, Rafael Muñoz Viana, Richard Pokorny, Margaret Ahmad^¶||, Robert Bittl, and Alfred Batschauer¹

From the Fachbereich Biologie-Pflanzenphysiologie, Philipps-Universität, Karl-von-Frisch-Strasse 8, 35032 Marburg, Germany, Freie Universität Berlin, Fachbereich Physik, Arnimallee 14, 14195 Berlin, Germany, ^¶Université Paris VI, Unité Mixte de Recherche-CNRS 7632, Tour 53E5, Casier 156, 4 Place Jussieu, 75252 Paris Cedex 05, France, and ^||Department of Biology, Penn State University, Media, Pennsylvania 19063

Cryptochrome (Cry) photoreceptors share high sequence and structural similarity with DNA repair enzyme DNA-photolyase and carry the same flavin cofactor. Accordingly, DNA-photolyase was considered a model system for the light activation process of cryptochromes. In line with this view were recent spectroscopic studies on cryptochromes of the CryDASH subfamily that showed photoreduction of the flavin adenine dinucleotide (FAD) cofactor to its fully reduced form. However, CryDASH members were recently shown to have photolyase activity for cyclobutane pyrimidine dimers in single-stranded DNA, which is absent for other members of the cryptochrome/photolyase family. Thus, CryDASH may have functions different from cryptochromes. The photocycle of other members of the cryptochrome family, such as Arabidopsis Cry1 and Cry2, which lack DNA repair activity but control photomorphogenesis and flowering time, remained elusive. Here we have shown that Arabidopsis Cry2 undergoes a photocycle in which semireduced flavin (FADH^·) accumulates upon blue light irradiation. Green light irradiation of Cry2 causes a change in the equilibrium of flavin oxidation states and attenuates Cry2-controlled responses such as flowering. These results demonstrate that the active form of Cry2 contains FADH^· (whereas catalytically active photolyase requires fully reduced flavin (FADH^-)) and suggest that cryptochromes could represent photoreceptors using flavin redox states for signaling differently from DNA-photolyase for photorepair.

Received for publication, January 22, 2007 , and in revised form, March 7, 2007.

^* This work was supported by the Deutsche Forschungsgemeinschaft (FOR 526, Grants BA985/10-1 and BA985/9-2 (to A. B.) and BI464/8-2 (to R. Bittl)) and a Ph.D. fellowship (GK "Protein function at the atomic level") from the same organization (to R. Banerjee). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1–3.

¹ To whom correspondence should be addressed: FB Biologie-Pflanzenphysiologie, Philipps-Universität, Karl-von-Frisch-Str. 8, 35032 Marburg, Germany. Tel.: 49-6421-282-7064; Fax: 49-6421-282-1545; E-mail: batschau{at}staff.uni-marburg.de.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C. T. Rodgers and P. J. Hore Chemical magnetoreception in birds: The radical pair mechanism PNAS, January 13, 2009; 106(2): 353 - 360. [Abstract] [Full Text] [PDF]

				X. Yu, R. Sayegh, M. Maymon, K. Warpeha, J. Klejnot, H. Yang, J. Huang, J. Lee, L. Kaufman, and C. Lin Formation of Nuclear Bodies of Arabidopsis CRY2 in Response to Blue Light Is Associated with Its Blue Light-Dependent Degradation PLANT CELL, January 1, 2009; 21(1): 118 - 130. [Abstract] [Full Text] [PDF]

				H. Liu, X. Yu, K. Li, J. Klejnot, H. Yang, D. Lisiero, and C. Lin Photoexcited CRY2 Interacts with CIB1 to Regulate Transcription and Floral Initiation in Arabidopsis Science, December 5, 2008; 322(5907): 1535 - 1539. [Abstract] [Full Text] [PDF]

				Compiled by, F. Tooke, T. Chiurugwi, and N. Battey Flowering Newsletter bibliography for 2007 J. Exp. Bot., July 18, 2008; (2008) ern109v1. [Full Text] [PDF]

				N. Ozturk, S.-H. Song, C. P. Selby, and A. Sancar Animal Type 1 Cryptochromes: ANALYSIS OF THE REDOX STATE OF THE FLAVIN COFACTOR BY SITE-DIRECTED MUTAGENESIS J. Biol. Chem., February 8, 2008; 283(6): 3256 - 3263. [Abstract] [Full Text] [PDF]

				N. Hoang, J.-P. Bouly, and M. Ahmad Evidence of a Light-Sensing Role for Folate in Arabidopsis Cryptochrome Blue-Light Receptors Mol Plant, January 1, 2008; 1(1): 68 - 74. [Abstract] [Full Text] [PDF]

				Y.-J. Yang, Z.-C. Zuo, X.-Y. Zhao, X. Li, J. Klejnot, Y. Li, P. Chen, S.-P. Liang, X.-H. Yu, X.-M. Liu, et al. Blue-Light-Independent Activity of Arabidopsis Cryptochromes in the Regulation of Steady-State Levels of Protein and mRNA Expression Mol Plant, January 1, 2008; 1(1): 167 - 177. [Abstract] [Full Text] [PDF]

				X. Yu, J. Klejnot, X. Zhao, D. Shalitin, M. Maymon, H. Yang, J. Lee, X. Liu, J. Lopez, and C. Lin Arabidopsis Cryptochrome 2 Completes Its Posttranslational Life Cycle in the Nucleus PLANT CELL, October 1, 2007; 19(10): 3146 - 3156. [Abstract] [Full Text] [PDF]

				S. Johnsen, E. Mattern, and T. Ritz Light-dependent magnetoreception: quantum catches and opponency mechanisms of possible photosensitive molecules J. Exp. Biol., September 15, 2007; 210(18): 3171 - 3178. [Abstract] [Full Text] [PDF]

				D. Immeln, R. Schlesinger, J. Heberle, and T. Kottke Blue Light Induces Radical Formation and Autophosphorylation in the Light-sensitive Domain of Chlamydomonas Cryptochrome J. Biol. Chem., July 27, 2007; 282(30): 21720 - 21728. [Abstract] [Full Text] [PDF]

				N. Ozturk, S.-H. Song, S. Ozgur, C. P. Selby, L. Morrison, C. Partch, D. Zhong, and A. Sancar Structure and Function of Animal Cryptochromes Cold Spring Harb Symp Quant Biol, January 1, 2007; 72(0): 119 - 131. [Abstract] [PDF]