Molecular evidence of the involvement of heat shock protein 90 in brassinosteroid signaling in Arabidopsis T87 cultured cells

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• 作者：Tomoaki Shigeta (1)
  Yuichi Zaizen (2)
  Tadao Asami (3)
  Shigeo Yoshida (4)
  Yasushi Nakamura (5)
  Shigehisa Okamoto (1)
  Tomoaki Matsuo (1)
  Yasushi Sugimoto (1)
  
• 关键词：Brassinosteroid ; Geldanamycin ; HSP90.3 ; BES1 ; CPD ; DWF4
• 刊名：Plant Cell Reports
• 出版年：2014
• 出版时间：March 2014
• 年：2014
• 卷：33
• 期：3
• 页码：499-510
• 全文大小：1,413 KB
• 作者单位：Tomoaki Shigeta (1)
  Yuichi Zaizen (2)
  Tadao Asami (3)
  Shigeo Yoshida (4)
  Yasushi Nakamura (5)
  Shigehisa Okamoto (1)
  Tomoaki Matsuo (1)
  Yasushi Sugimoto (1)
  
  1. The United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan
  2. Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan
  3. Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan
  4. Kihara Institute for Biological Research, Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama, 244-0813, Japan
  5. Department of Food Sciences and Nutritional Health, Kyoto Prefectural University, Shimogamo-Hangi-cho, Sakyo-ku, Kyoto, 606-8522, Japan
  
• ISSN：1432-203X

文摘

Key message A closer association of HSP90s with brassinosteroid signaling is suggested by the brassinosteroid-triggered formation of an HSP90-containing macromolecular complex and the direct interaction between HSP90.3 and BES1. Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that is reportedly involved in the proper folding, stabilization, intracellular trafficking, maintenance and degradation of numerous proteins, as well as the facilitation of cellular signaling in various organisms including plants. Brassinosteroids (BRs), a class of unique steroidal hormones, play crucial roles in plant growth and development. The interaction between HSP90 proteins and BR action has been poorly understood. Here, we present molecular evidence suggesting that HSP90 proteins have a function(s) in BR signal transduction. First, blue native/sodium dodecyl sulfate-polyacrylamide gel electrophoresis linked immunoblotting demonstrated that a bioactive BR, brassinolide (BL), promotes the formation of some HSP90-containing macromolecular complexes with molecular weight more than 480?kDa in Arabidopsis T87 cultured cells. Second, HSP90.3, one of seven Arabidopsis HSP90 family proteins, was observed to interact in vitro with BRI1-EMS-SUPPRESSOR 1 (BES1), a transcription factor acting in BR signaling. Geldanamycin, an inhibitor of ATPase activity in HSP90, not only diminished HSP90.3 interaction with BES1 in vitro, but also suppressed BL-induced down-regulation of two BR biosynthesis genes, CONSTITUTIVE PHOTHOMORPHOGENESIS AND DWARFISM and DWARF4 in vivo. The results suggest the involvement of the HSP90/BES1 heterocomplexes in BR signaling-mediated feedback control in BR contents. Together, our results provide important clues to elucidate HSP90s-functions in the BR signaling pathway in Arabidopsis.