Binding of the Maize Cytosolic Hsp70 to Calmodulin, and Identification of Calmodulin-Binding Site in Hsp70^1
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概要
- 論文の詳細を見る
Using a gel-overlay technique of biotinylated calmodulin(CaM), we showed that maize cytosolic Hsp70 protein could bind to CaM in the presence of 1 mM CaCl_2. The purified maize cytosolic Hsp70 inhibited the activity of CaM-dependent NADK in a concentration-dependent manner. A synthetic peptide, which possesses the 21 amino acid sequence, PRALRRLRTACERAKRTLSST, at positions 261-281 in maize cytosolic Hsp70, could associate with CaM in the presence of 1 mM calcium. The synthetic peptide inhibited CaM-dependent NADK activity and PDE activity. This indicates that the 21-amino acid sequence at positions 261-281 is the CaM-binding site. The binding of CaM to Hsp70 inhibited the ATPase activity of Hsp70. The possible regulator function of Hsp70 in cell signaling events in response to heat stress is discussed.
- 日本植物生理学会の論文
著者
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Zhou Ren-gang
Institute Of Molecular Cell Biology Hebei Normal University
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LI Bing
Institute of Computer Science and Engineering, Beijing Jiaotong University
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Li Bing
Institute Of Computer Science And Engineering Beijing Jiaotong University
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Li Bing
Institute Of Molecular Cell Biology Hebei Normal University
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Sun Xu-tong
Institute of Agro-physics, Physiology and Biochemistry, Hebei Academy of Agricultural Sciences
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Zhou Gou-min
Institute of Biochemistry, The Chinese Academy of Sciences
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Tang Wen-qiang
Biology Department, Hebei Normal University
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Bai Juan
Biology Department, Hebei Normal University
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Sun Da-ye
Biology Department, Hebei Normal University
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Tang Wen-qiang
Biology Department Hebei Normal University
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Sun D‐y
Institute Of Molecular Cell Biology Hebei Normal University
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Sun Xu-tong
Institute Of Agro-physics Physiology And Biochemistry Hebei Academy Of Agricultural Sciences:biology
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Zhou Gou-min
Institute Of Biochemistry The Chinese Academy Of Sciences
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Bai Juan
Biology Department Hebei Normal University
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