title: N-Terminal acetylation is critical for forming α-helical oligomer of α-synuclein.
abstract: The aggregation of the protein α-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 α-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 α-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.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
authors.forename: Adam J
authors.initials: AJ
authors.lastname: Trexler
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Rhoades
mesh_terms: D000107:Acetylation; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D002850:Chromatography, Gel; D002942:Circular Dichroism; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization; D051844:alpha-Synuclein / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000682:Amyloid; D011994:Recombinant Proteins; C497604:SNCA protein, human; D051844:alpha-Synuclein