A Disulfide Bridge Mediated by Cysteine 574 Is Formed in the Dimer of the 70-kDa Heat Shock Protein

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著者

    • Nemoto Takayuki K. NEMOTO Takayuki K.
    • Division of Oral Molecular Biology, Department of Developmental and Reconstructive Medicine, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences
    • Fukuma Yutaka FUKUMA Yutaka
    • Division of Oral Molecular Biology, Department of Developmental and Reconstructive Medicine, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences
    • Itoh Hideaki [他] ITOH Hideaki
    • Department of Material-Process Engineering and Applied Chemistry for Environment, Akita University Faculty of Engineering and Resource Science
    • TAKAGI Takashi
    • Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences, Tohoku University
    • ONO Toshio
    • Division of Oral Molecular Biology, Department of Developmental and Reconstructive Medicine, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences

抄録

The 70-kDa heat shock protein (Hsp70) is predominantly present intracellularly as a monomer, but a small population is converted to dimers and oligomers under certain conditions. In the present study, we investigated the dimeric structure of human inducible Hsp70. As reported earlier, the C-terminal client-binding domain (amino acids 382-641) was required for the dimerization. A 40-amino acid deletion in the client-binding domain from either the N-terminus or C-terminus greatly enhanced the dimerization potential of Hsp70. Limited proteolysis indicated that the dimer formed through truncation from the C-terminus had a conformation similar to that of the non-truncated form. Truncation experiments demonstrated that the client-binding sub-domain (amino acids 382-520) with its adjacent region up to amino acid 541 was not sufficient for the dimerization but that the region up to amino acid 561 was sufficient. Interestingly, the dimer formed through truncation from the C-terminus acquired a homomeric disulfide bridge at Cys574.

収録刊行物

  • The journal of biochemistry  

    The journal of biochemistry 139(4), 677-687, 2006-04-01 

    Japanese Biochemical Society

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各種コード

  • NII論文ID(NAID)
    10018845511
  • NII書誌ID(NCID)
    AA00694073
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    0021924X
  • NDL 記事登録ID
    7912421
  • NDL 雑誌分類
    ZR2(科学技術--生物学--生化学)
  • NDL 請求記号
    Z53-B472
  • データ提供元
    CJP書誌  NDL  IR 
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