Plant Physiol. Drug Metab Dispos
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Published on September 28, 2007; 10.1104/pp.107.104844

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Received June 30, 2007
Accepted September 17, 2007

Genetic Characterization of Mutants Resistant to the Antiauxin p-chlorophenoxyisobutyric Acid (PCIB) Reveals that AAR3, a Gene Encoding DCN1-Like Protein, regulates responses to the synthetic auxin 2,4-dichlorophenoxyacetic acid in Arabidopsis roots

Kamal Kanti Biswas , Chiharu Ooura , Kanako Higuchi , Yuji Miyazaki , Vinh Van Nguyen , Abidur Rahman , Hirofumi Uchimiya , Tomohiro Kiyosue , Tomokazu Koshiba , Atsushi Tanaka , Issay Narumi , and Yutaka Oono *

Radiation-Applied Biology Division, Japan Atomic Energy Agency, Takasaki, 370-1292, Japan; Advanced Science Research Center, Japan Atomic Energy Research Institute, Takasaki 370-1292, Japan; Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan; United Graduate School of Agricultural Sciences, Ehime University Matsuyama, Ehime 790-8566, Japan; Biology Department, University of Massachusetts, Amherst, MA-01003, USA; Institute of Research Promotion, Kagawa University, Kagawa 761-0795, Japan; Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan

* Corresponding author; email: ohno.yutaka{at}jaea.go.jp.

To isolate novel auxin-responsive mutants in Arabidopsis, 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 5 independent loci including two known auxin-related loci, TIR1 and AtCUL1. 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 (DCN-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.




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