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First published online January 13, 2006; 10.1104/pp.105.071282

Plant Physiology 140:844-855 (2006)
© 2006 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

G-Protein-Coupled Receptor 1, G-Protein G{alpha}-Subunit 1, and Prephenate Dehydratase 1 Are Required for Blue Light-Induced Production of Phenylalanine in Etiolated Arabidopsis1

Katherine Mary Warpeha, Syed Salman Lateef, Yevgeniya Lapik, Marybeth Anderson, Bao-Shiang Lee and Lon Seth Kaufman*

Laboratory for Molecular Biology, Department of Biological Sciences (K.M.W., M.A., L.S.K.), Protein Research Laboratory, Research Resources Center (S.S.L., B.-S.L.), and Department of Biochemistry and Genetics (Y.L.), University of Illinois, Chicago, Illinois 60607

Different classes of plant hormones and different wavelengths of light act through specific signal transduction mechanisms to coordinate higher plant development. A specific prephenate dehydratase protein (PD1) was discovered to have a strong interaction with the sole canonical G-protein G{alpha}-subunit (GPA1) in Arabidopsis (Arabidopsis thaliana). PD1 is a protein located in the cytosol, present in etiolated seedlings, with a specific role in blue light-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe). Insertion mutagenesis confirms that GPA1 and the sole canonical G-protein-coupled receptor (GCR1) in Arabidopsis also have a role in this blue light-mediated event. In vitro analyses indicate that the increase in PD1 activity is the direct and specific consequence of its interaction with activated GPA1. Because of their shared role in the light-mediated synthesis of phenylpyruvate and Phe, because they are iteratively interactive, and because activated GPA1 is directly responsible for the activation of PD1; GCR1, GPA1, and PD1 form all of or part of a signal transduction mechanism responsible for the light-mediated synthesis of phenylpyruvate, Phe, and those metabolites that derive from that Phe. Data are also presented to confirm that abscisic acid can act through the same pathway. An additional outcome of the work is the confirmation that phenylpyruvate acts as the intermediate in the synthesis of Phe in etiolated plants, as it commonly does in bacteria and fungi.

1 This work was supported by the U.S. Department of Agriculture (grant no. CREES 2005–02389 to L.S.K.).

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Lon Seth Kaufman (lkaufman{at}uic.edu).

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.071282.

* Corresponding author; e-mail lkaufman{at}uic.edu; fax 312–413–2691.

Received September 12, 2005; returned for revision December 15, 2005; accepted December 19, 2005.




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