Genetic Characterization of Mutants Resistant to the Antiauxinp-Chlorophenoxyisobutyric Acid Reveals ThatAAR3, a Gene Encoding a DCN1-Like Protein, Regulates Responses to the Synthetic Auxin 2,4-Dichlorophenoxyacetic Acid in Arabidopsis Roots | Zendy

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

Open Access

Genetic Characterization of Mutants Resistant to the Antiauxinp-Chlorophenoxyisobutyric Acid Reveals ThatAAR3, a Gene Encoding a DCN1-Like Protein, Regulates Responses to the Synthetic Auxin 2,4-Dichlorophenoxyacetic Acid in Arabidopsis Roots

Author(s) -

Kamal Kanti Biswas,

Chiharu Ooura,

Kanako Higuchi,

Yuji Miyazaki,

Vinh Van Nguyen,

Abidur Rahman,

Hirofumi Uchimiya,

Tomohiro Kiyosue,

Tomokazu Koshiba,

Atsushi Tanaka,

Issay Narumi,

Yutaka Oono

Publication year - 2007

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.107.104844

Subject(s) - mutant , gene , biology , auxin , genetics

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.

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