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First published online September 28, 2007; 10.1104/pp.107.104844 Plant Physiology 145:773-785 (2007) © 2007 American Society of Plant Biologists Genetic Characterization of Mutants Resistant to the Antiauxin p-Chlorophenoxyisobutyric Acid Reveals That AAR3, a Gene Encoding a DCN1-Like Protein, Regulates Responses to the Synthetic Auxin 2,4-Dichlorophenoxyacetic Acid in Arabidopsis Roots1,[C],[W]Radiation-Applied Biology Division, Japan Atomic Energy Agency, Takasaki 370–1292, Japan (K.K.B., V.V.N., A.R., A.T., I.N., Y.O.); Advanced Science Research Center, Japan Atomic Energy Research Institute, Takasaki 370–1292, Japan (C.O., H.U., Y.O.); Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University, Hachioji, Tokyo 192–0397, Japan (K.H., T. Koshiba); United Graduate School of Agricultural Sciences, Ehime University, Matsuyama, Ehime 790–8566, Japan (Y.M., T. Kiyosue); Biology Department, University of Massachusetts, Amherst, Massachusetts 01003 (A.R.); Institute of Molecular and Cellular Biosciences, University of Tokyo, Tokyo 113–0032, Japan (H.U.); and Institute of Research Promotion, Kagawa University, Kagawa 761–0795, Japan (T. Kiyosue)
To isolate novel auxin-responsive mutants in Arabidopsis (Arabidopsis thaliana), we screened mutants for root growth resistance to a putative antiauxin, p-chlorophenoxyisobutyric acid (PCIB), which inhibits auxin action by interfering the upstream auxin-signaling events. Eleven PCIB-resistant mutants were obtained. Genetic mapping indicates that the mutations are located in at least five independent loci, including two known auxin-related loci, TRANSPORT INHIBITOR RESPONSE1 and Arabidopsis CULLIN1. antiauxin-resistant mutants (aars) aar3-1, aar4, and aar5 were also resistant to 2,4-dichlorophenoxyacetic acid as shown by a root growth assay. Positional cloning of aar3-1 revealed that the AAR3 gene encodes a protein with a domain of unknown function (DUF298), which has not previously been implicated in auxin signaling. The protein has a putative nuclear localization signal and shares homology with the DEFECTIVE IN CULLIN NEDDYLATION-1 protein through the DUF298 domain. The results also indicate that PCIB can facilitate the identification of factors involved in auxin or auxin-related signaling.
1 This work was supported in part by the Japan Society for the Promotion of Science (Postdoctoral Fellowship for Foreign Researchers to K.K.B. and A.R.) and the Ministry of Education, Culture, Sports, Science and Technology of Japan (Grants-in-Aid for Scientific Research [KAKENHI; nos. 17084003 to T. Kiyosue and 16570042 to Y.O.] and the Nuclear Researchers Exchange Program [for V.V.N.]). 2 Present address: Department of Biological Sciences, Simon Fraser University, Burnaby, BC, Canada V5A 1S6. 3 Present address: Research Development Division, Fujirebio Inc., Hachioji, Tokyo 192–0031, Japan. 4 Present address: Department of Science-Technology and Co-operation, Ho Chi Minh University of Industry, Ho Chi Minh City, Vietnam. 5 Present address: Cryobiosystem Research Center, Faculty of Agriculture, Iwate University, Ueda, Morioka 020–8550, Japan. 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: Yutaka Oono (ohno.yutaka{at}jaea.go.jp). [C] Some figures in this article are displayed in color online but in black and white in the print edition. [W] The online version of this article contains Web-only data. www.plantphysiol.org/cgi/doi/10.1104/pp.107.104844 * Corresponding author; e-mail ohno.yutaka{at}jaea.go.jp. Received June 30, 2007; accepted September 17, 2007; published September 28, 2007. This article has been cited by other articles:
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