Chaperone-like activities of α-synuclein: α-Synuclein assists enzyme activities of esterases

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• 作者：Misun Ahn ; SeungBum Kim ; Mira Kang ; Yeonwoo Ryu and T. Doohun Kim
• 关键词：Microbial esterases ; α ; -Synuclein ; Intrinsically unstructured
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2006
• 出版时间：11 August 2006
• 年：2006
• 卷：346
• 期：4
• 页码：1142-1149
• 全文大小：574 K

文摘

α-Synuclein, a major constituent of Lewy bodies (LBs), has been implicated to play a critical role in the pathogenesis of Parkinson’s disease (PD), although the physiological function of α-synuclein has not yet been known. Here we have shown that α-synuclein, which has no well-defined secondary or tertiary structure, can protect the enzyme activity of microbial esterases against stress conditions such as heat, pH, and organic solvents. In particular, the flexibility of α-synuclein and its C-terminal region seems to be important for complex formation, but the structural integrity of the C-terminal region may not be required for stabilization of enzyme activity. In addition, atomic force microscopy (AFM) and in vivo enzyme assays showed highly specific interactions of esterases with α-synuclein. Our results indicate that α-synuclein not only protects the enzyme activity of microbial esterases in vitro, but also can stabilize the active conformation of microbial esterases in vivo.