Formation and Dissociation of the BSS1 Protein Complex Regulates Plant Development via Brassinosteroid Signaling. Issue 2 (6th February 2015)
- Record Type:
- Journal Article
- Title:
- Formation and Dissociation of the BSS1 Protein Complex Regulates Plant Development via Brassinosteroid Signaling. Issue 2 (6th February 2015)
- Main Title:
- Formation and Dissociation of the BSS1 Protein Complex Regulates Plant Development via Brassinosteroid Signaling
- Authors:
- Shimada, Setsuko
Komatsu, Tomoyuki
Yamagami, Ayumi
Nakazawa, Miki
Matsui, Minami
Kawaide, Hiroshi
Natsume, Masahiro
Osada, Hiroyuki
Asami, Tadao
Nakano, Takeshi - Abstract:
- Abstract : BSS1 forms a complex with a master regulator of brassinosteroid signaling, thereby restricting the regulator to the cytosol and negatively regulating brassinosteroid signaling. Abstract: 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 -overexpressingAbstract : BSS1 forms a complex with a master regulator of brassinosteroid signaling, thereby restricting the regulator to the cytosol and negatively regulating brassinosteroid signaling. Abstract: 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. … (more)
- Is Part Of:
- The Plant Cell. Volume 27:Issue 2(2015)
- Journal:
- The Plant Cell
- Issue:
- Volume 27:Issue 2(2015)
- Issue Display:
- Volume 27, Issue 2 (2015)
- Year:
- 2015
- Volume:
- 27
- Issue:
- 2
- Issue Sort Value:
- 2015-0027-0002-0000
- Page Start:
- 375
- Page End:
- 390
- Publication Date:
- 2015-02-06
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.114.131508 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
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- 16318.xml