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Science 27 November 1998:
Vol. 282. no. 5394, pp. 1698 - 1701
DOI: 10.1126/science.282.5394.1698
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Reports

Arabidopsis NPH1: A Flavoprotein with the Properties of a Photoreceptor for Phototropism

John M. Christie, Philippe Reymond, Gary K. Powell, Paul Bernasconi, Andrei A. Raibekas, Emmanuel Liscum, Winslow R. Briggs *

The NPH1 gene of Arabidopsis thaliana encodes a 120-kilodalton serine-threonine protein kinase hypothesized to function as a photoreceptor for phototropism. When expressed in insect cells, the NPH1 protein is phosphorylated in response to blue light irradiation. The biochemical and photochemical properties of the photosensitive protein reflect those of the native protein in microsomal membranes. Recombinant NPH1 noncovalently binds flavin mononucleotide, a likely chromophore for light-dependent autophosphorylation. The fluorescence excitation spectrum of the recombinant protein is similar to the action spectrum for phototropism, consistent with the conclusion that NPH1 is an autophosphorylating flavoprotein photoreceptor mediating phototropic responses in higher plants.

J. M. Christie and W. R. Briggs, Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305, USA. P. Reymond, Institut de Biologie et de Physiologie Végétales, Université de Lausanne, 1015 Lausanne, Switzerland. G. K. Powell and P. Bernasconi, Novartis Agribusiness Biotechnology Research Inc., 3054 Cornwallis Road, Research Triangle Park, NC 27709, USA. A. A. Raibekas, Department of Biological Chemistry, University of Michigan, M5416 Medical Science I, Ann Arbor, MI 48109, USA. E. Liscum, Division of Biological Sciences, University of Missouri, Columbia, MO 65211, USA.
*   To whom correspondence should be addressed. E-mail: briggs{at}andrew.stanford.edu

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