Formation and Dissociation of the BSS1 Protein Complex Regulates Plant Development via Brassinosteroid Signaling
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- Setsuko Shimada
- Antibiotics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan
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- Tomoyuki Komatsu
- Antibiotics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan
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- Ayumi Yamagami
- Antibiotics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan
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- Miki Nakazawa
- RIKEN Genome Science Center, Tsurumi, Yokohama, Kanagawa 230-0045, Japan
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- Minami Matsui
- Synthetic Genomics Research Team, Biomass Engineering Program Cooperation Division, RIKEN Center for Sustainable Resource Science, Tsurumi, Yokohama, Kanagawa 230-0045, Japan
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- Hiroshi Kawaide
- United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Saiwai-Cho, Fuchu, Tokyo 183-8509, Japan
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- Masahiro Natsume
- United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Saiwai-Cho, Fuchu, Tokyo 183-8509, Japan
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- Hiroyuki Osada
- Antibiotics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan
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- Tadao Asami
- Department of Applied Biological Chemistry, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
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- Takeshi Nakano
- Antibiotics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan
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説明
<jats:title>Abstract</jats:title> <jats:p>Brassinosteroids (BRs) play important roles in plant development and the response to environmental cues. BIL1/BZR1 is a master transcription factor in BR signaling, but the mechanisms that lead to the finely tuned targeting of BIL1/BZR1 by BRs are unknown. Here, we identified BRZ-SENSITIVE-SHORT HYPOCOTYL1 (BSS1) as a negative regulator of BR signaling in a chemical-biological analysis involving brassinazole (Brz), a specific BR biosynthesis inhibitor. The bss1-1D mutant, which overexpresses BSS1, exhibited a Brz-hypersensitive phenotype in hypocotyl elongation. BSS1 encodes a BTB-POZ domain protein with ankyrin repeats, known as BLADE ON PETIOLE1 (BOP1), which is an important regulator of leaf morphogenesis. The bss1-1D mutant exhibited an increased accumulation of phosphorylated BIL1/BZR1 and a negative regulation of BR-responsive genes. The number of fluorescent BSS1/BOP1-GFP puncta increased in response to Brz treatment, and the puncta were diffused by BR treatment in the root and hypocotyl. We show that BSS1/BOP1 directly interacts with BIL1/BZR1 or BES1. The large protein complex formed between BSS1/BOP1 and BIL1/BZR1 was only detected in the cytosol. The nuclear BIL1/BZR1 increased in the BSS1/BOP1-deficient background and decreased in the BSS1/BOP1-overexpressing background. Our study suggests that the BSS1/BOP1 protein complex inhibits the transport of BIL1/BZR1 to the nucleus from the cytosol and negatively regulates BR signaling.</jats:p>
収録刊行物
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- The Plant Cell
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The Plant Cell 27 (2), 375-390, 2015-02-01
Oxford University Press (OUP)