Alpha-synuclein has structural and functional similarities to small heat shock proteins |
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Authors: | Kim Thomas Doohun Choi Eunjin Rhim Hyangshuk Paik Seung R Yang Chul-Hak |
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Affiliation: | a School of Chemistry and Molecular Engineering, Seoul National University, Seoul, Republic of Korea b Department of Molecular Biology, Catholic University Medical College, Seoul, Republic of Korea c School of Chemical Engineering, Seoul National University, Seoul, Republic of Korea |
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Abstract: | The aggregation and fibrillization of α-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 α-synuclein is not yet clearly elucidated. Here, we showed that C-terminal region of α-synuclein is similar to α-crystalline domain of small heat shock proteins. In our experiments, α-synuclein, like small heat shock proteins, protected cellular proteins from denaturation, and confer Escherichia coli cellular tolerances against thermal- and oxidative-stresses. |
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Keywords: | α-Synuclein Small heat shock protein Parkinson&rsquo s disease |
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