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The aggregation of α-synuclein is believed to play an important role in the pathogenesis of Parkinson's disease as well as other neurodegenerative disorders (“synucleinopathies”). However, the function of α-synuclein under physiologic and pathological conditions is unknown, and the mechanism of α-synuclein aggregation is not well understood. Here we show that α-synuclein forms a tight 2:1 complex with histones and that the fibrillation rate of α-synuclein is dramatically accelerated in the presence of histones in vitro. We also describe the presence of α-synuclein and its co-localization with histones in the nuclei of nigral neurons from mice exposed to a toxic insult (i.e., injections of the herbicide paraquat). These observations indicate that translocation into the nucleus and binding with histones represent potential mechanisms underlying α-synuclein pathophysiology.