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. 2019 Jul 29;9:10919. doi: 10.1038/s41598-019-47227-z

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Alpha-synuclein binds double-stranded DNA and facilitates the DNA non-homologous end-joining reaction. (A) Left: EMSA of shifted 300 bp dsDNA run on a 6% polyacrylamide gel with increasing alpha-synuclein (αSyn) shows at least 6 different bound states (white arrowheads). Right: Integrated density of each band plotted versus distance on the gel shows progressive reduction of the unshifted peak (black arrowhead) and simultaneous increase in the multiple shifted peaks (white arrowheads) with increasing αSyn concentration. (B) Left: Similar EMSA with S129-phospho-synuclein (pSyn) shows only 2 different bound states (white arrowheads). Right: Integrated density of each band plotted versus gel distance shows similar, but fewer, shifted peaks (white arrowheads) with increasing pSyn concentration, also associated with a reduction of the unshifted peak (black arrowhead). (C) Left: DNA T4 ligase-mediated non-homologous end-joining assay shows formation of ligation products, including dimer band (red arrowhead) and circularized monomer (white arrowhead), with two concentrations of pSyn compared to GFP (negative control) and histone H1 (positive control). Right: Group data shows a significant difference between control and pSyn and αSyn for both the dimerization and circularized monomer products (dimerization ratio versus T4 ligase-only condition: 0.7 μm protein GFP = 0.76 ± 0.11, N = 6; pSyn = 2.33 ± 0.23, N = 10, αSyn = 3.04 ± 0.37, N = 6, F(2, 19) = 16.77, p < 0.0001, ANOVA, post-hoc Tukey test: GFP vs. pSyn p = 0.0011, GFP vs. αSyn p < 0.0001, pSyn vs. αSyn p = 0.1450; 3.6 μm protein GFP = 1.21 ± 0.19, N = 4; pSyn = 3.40 ± 0.53, N = 7, t-test p = 0.0154; circularization ratio versus T4 ligase-only condition: 0.7 μm protein GFP = 1.23 ± 0.20, N = 6; pSyn = 2.91 ± 0.30, N = 10, αSyn = 3.05 ± 0.28, N = 6, F(2, 19) = 10.77, p = 0.0007, ANOVA, post-hoc Tukey test: GFP vs. pSyn p = 0.0015, GFP vs. αSyn p = 0020, pSyn vs. αSyn p = 0.9349; 3.6 μm protein GFP = 1.21 ± 0.19, N = 4; pSyn = 3.40 ± 0.53, N = 7, t-test p = 0.0007).