Structural changes in α-synuclein affect its chaperone-like activity in vitroStructural changes in alpha-synuclein affect its chaperone-like activity in vitro
- Other Titles
- Structural changes in alpha-synuclein affect its chaperone-like activity in vitro
- Authors
- Kim, Doo Hun; Paik, Seung R.; Yang, Chul-Hak; Kim, Jongsun
- Issue Date
- Dec-2000
- Publisher
- The Protein Society
- Citation
- Protein Science, v.9, no.12, pp 2489 - 2496
- Pages
- 8
- Journal Title
- Protein Science
- Volume
- 9
- Number
- 12
- Start Page
- 2489
- End Page
- 2496
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159251
- DOI
- 10.1110/ps.9.12.2489
- ISSN
- 0961-8368
1469-896X
- Abstract
- α-Synuclein, a major constituent of Lewy bodies (LBs) in Parkinson's disease (PD), has been implicated to play a critical role in synaptic events, such as neuronal plasticity during development, learning, and degeneration under pathological conditions, although the physiological function of α-synuclein has not yet been established. We here present biochemical evidence that recombinant α-synuclein has a chaperone-like function against thermal and chemical stress in vitro. In our experiments, α-synuclein protected glutathione S-transferase (GST) and aldolase from heat-induced precipitation, and α-lactalbumin and bovine serum albumin from dithiothreitol (DTT)-induced precipitation like other molecular chaperones. Moreover, preheating of α-synuclein, which is believed to reorganize the molecular surface of α-synuclein, increased the chaperone-like activity. Interestingly, in organic solvents, which promotes the formation of secondary structure, α-synuclein aggregated more easily than in its native condition, which eventually might abrogate the chaperone-like function of the protein. In addition, α-synuclien was also rapidly and significantly precipitated by heat in the presence of Zn2+ in vitro, whereas it was not affected by the presence of Ca2+ or Mg2+. Circular dichroism spectra confirmed that α-synuclein underwent conformational change in the presence of Zn2+. Taken together, our data suggest that α-synuclein could act as a molecular chaperone, and that the conformational change of the α-synuclein could explain the aggregation kinetics of α-synuclein, which may be related to the abolishment of the chaperonic-like activity.
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