Plant Physiology Preview
Published on May 24, 2002; 10.1104/pp.010969
Received October 23, 2001
Returned for revision December 26, 2001
Accepted March 12, 2002
Action Spectrum for Cryptochrome-Dependent Hypocotyl Growth
Inhibition in Arabidopsis
Margaret Ahmad *, Nicholas Grancher , Mary Heil , Robert C. Black , Baldissera Giovani , Paul Galland , and Danielle Lardemer
Universite Paris VI, Tour 53 E 5, Casier 156, 4, Place Jussieu, 75252 Paris cedex 05, France (M.A., N.G., B.G., D.L.); Pennsylvania State University, 25 Yearsley Mill Road, Media, Pennsylvania 19063 (M.A., M.H., R.C.B.); and FB Biologie/Botanik, Philipps-Universitaet Marburg, Karl-von-Frisch-Strasse, 35032 Marburg, Germany (P.G.)
* Corresponding author; email: ahmad{at}ccr.jussieu.fr.
Cryptochrome blue-light photoreceptors are found in both plants and animals and have been implicated in numerous developmental and circadian signaling pathways. Nevertheless, no action spectrum for a physiological response shown to be entirely under the control of cryptochrome has been reported. In this work, an action spectrum was determined in vivo for a cryptochrome-mediated high-irradiance response, the blue-light-dependent inhibition of hypocotyl elongation in Arabidopsis. Comparison of growth of wild-type, cry1cry2 cryptochrome-deficient double mutants, and cryptochrome-overexpressing seedlings demonstrated that responsivity to monochromatic light sources within the range of 390 to 530 nm results from the activity of cryptochrome with no other photoreceptor having a significant primary role at the fluence range tested. In both green- and norflurazon-treated (chlorophyll-deficient) seedlings, cryptochrome activity is fairly uniform throughout its range of maximal response (390--480 nm), with no sharply defined peak at 450 nm; however, activity at longer wavelengths was disproportionately enhanced in CRY1-overexpressing seedlings as compared with wild type. The action spectrum does not correlate well with the absorption spectra either of purified recombinant cryptochrome photoreceptor or to that of a second class of blue-light photoreceptor, phototropin (PHOT1 and PHOT2). Photoreceptor concentration as determined by western-blot analysis showed a greater stability of CRY2 protein under the monochromatic light conditions used in this study as compared with broad band blue light, suggesting a complex mechanism of photoreceptor activation. The possible role of additional photoreceptors (in particular phytochrome A) in cryptochrome responses is discussed.
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