N-Terminal acetylation is critical for forming alpha-helical oligomer of alpha-synuclein.
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Trexler AJ, Rhoades E
N-Terminal acetylation is critical for forming alpha-helical oligomer of alpha-synuclein.
Protein Sci. 2012 May;21(5):601-5. doi: 10.1002/pro.2056. Epub 2012 Mar 30.
- PubMed ID
- 22407793 [ View in PubMed]
- Abstract
The aggregation of the protein alpha-synuclein (AS) is critical to the pathogenesis of Parkinson's disease. Although generally described as an unstructured monomer, recent evidence suggests that the native form of AS may be an alpha-helical tetramer which resists aggregation. Here, we show that N-terminal acetylation in combination with a mild purification protocol results in an oligomeric form of AS with partial alpha-helical structure. N-terminal acetylation of AS could have important implications for both the native and pathological structures and functions of AS. Through our demonstration of a recombinant expression system, our results represent an important step toward biochemical and biophysical characterization of this potentially important form of AS.