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Plant Physiol, December 2000, Vol. 124, pp. 1728-1738

Aux/IAA Proteins Are Phosphorylated by Phytochrome in Vitro1

Adán Colón-Carmona,2 Donna L. Chen, Kuo-Chen Yeh,3 and Steffen Abel*

Department of Vegetable Crops (A.C.-C., D.L.C., S.A.) and Section of Molecular and Cellular Biology (K.-C.Y.), University of California, One Shields Avenue, Davis, California 95616

Auxin/indole-3-acetic acid (Aux/IAA) genes encode short-lived transcription factors that are induced as a primary response to the plant growth hormone IAA or auxin. Gain-of-function mutations in Arabidopsis genes, SHY2/IAA3, AXR3/IAA17, and AXR2/IAA7 cause pleiotropic phenotypes consistent with enhanced auxin responses, possibly by increasing Aux/IAA protein stability. Semidominant mutations shy2-1D, shy2-2, axr3-1, and axr2-1 induce ectopic light responses in dark-grown seedlings. Because genetic studies suggest that the shy2-1D and shy2-2 mutations bypass phytochrome requirement for certain aspects of photomorphogenesis, we tested whether SHY2/IAA3 and related Aux/IAA proteins interact directly with phytochrome and whether they are substrates for its protein kinase activity. Here we show that recombinant Aux/IAA proteins from Arabidopsis and pea (Pisum sativum) interact in vitro with recombinant phytochrome A from oat (Avena sativa). We further show that recombinant SHY2/IAA3, AXR3/IAA17, IAA1, IAA9, and Ps-IAA4 are phosphorylated by recombinant oat phytochrome A in vitro. Deletion analysis of Ps-IAA4 indicates that phytochrome A phosphorylation occurs on the N-terminal half of the protein. Metabolic labeling and immunoprecipitation studies with affinity-purified antibodies to IAA3 demonstrate increased in vivo steady-state levels of mutant IAA3 in shy2-2 plants and phosphorylation of the SHY2-2 protein in vivo. Phytochrome-dependent phosphorylation of Aux/IAA proteins is proposed to provide one molecular mechanism for integrating auxin and light signaling in plant development.

1 This work was supported by the U.S. Department of Agriculture National Research Initiative Competitive Grants Program (grant no. 9801409 to S.A.).

2 Present address: Department of Biology, University of Massachusetts, Boston, MA 02125.

3 Present address: Department of Biological Sciences, Stanford University, Stanford, CA 94305.

* Corresponding author; email sabel{at}ucdavis.edu; fax 530- 752-9659.

© 2000 American Society of Plant Physiologists


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