α-突触核蛋白与小分子热休克蛋白在结构和功能上具有相似性。
Alpha-synuclein has structural and functional similarities to small heat shock proteins.
作者信息
Kim Thomas Doohun, Choi Eunjin, Rhim Hyangshuk, Paik Seung R, Yang Chul-Hak
机构信息
School of Chemistry and Molecular Engineering, Seoul National University, Seoul, Republic of Korea.
出版信息
Biochem Biophys Res Commun. 2004 Nov 26;324(4):1352-9. doi: 10.1016/j.bbrc.2004.09.208.
The aggregation and fibrillization of alpha-synuclein, a major component of Lewy bodies, is a key event in Parkinson's disease. Although the mechanisms of fibrils formation are largely investigated, physiological function of alpha-synuclein is not yet clearly elucidated. Here, we showed that C-terminal region of alpha-synuclein is similar to alpha-crystalline domain of small heat shock proteins. In our experiments, alpha-synuclein, like small heat shock proteins, protected cellular proteins from denaturation, and confer Escherichia coli cellular tolerances against thermal- and oxidative-stresses.
α-突触核蛋白是路易小体的主要成分，其聚集和纤维化是帕金森病中的关键事件。尽管对纤维形成机制进行了大量研究，但α-突触核蛋白的生理功能尚未明确阐明。在此，我们表明α-突触核蛋白的C末端区域与小分子热休克蛋白的α-晶体结构域相似。在我们的实验中，α-突触核蛋白与小分子热休克蛋白一样，保护细胞蛋白质免于变性，并赋予大肠杆菌细胞对热应激和氧化应激的耐受性。
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