Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step Mechanism

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• 作者：Graumann ; Johannes ; Lilie ; Hauke ; Tang ; Xianli ; Tucker ; Katherine A. ; Hoffmann ; Jö ; rg H. ; et. al.
• 关键词：dimerization ; disulfide bond formation ; heat shock protein ; oxidative stress ; redox regulation ; structure
• 刊名：Structure
• 出版年：2001
• 出版时间：May, 2001
• 年：2001
• 卷：9
• 期：5
• 页码：377-387
• 全文大小：360 K

文摘

Background: Hsp33 is a novel redox-regulated molecular chaperone. Hsp33 is present in the reducing environment of the cytosol and is, under normal conditions, inactive. The four highly conserved cysteines found in Hsp33 constitute a novel zinc binding motif. Upon exposure to oxidative stress, Hsp33's chaperone activity is turned on. This activation process is initiated by the formation of two intramolecular disulfide bonds. Recently, the 2.2 Å crystal structure of Hsp33 has been solved, revealing that Hsp33 is present as a dimer in the structure (Vijayalakshmi et al., this issue, 367–375 ).