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. Author manuscript; available in PMC: 2021 May 11.
Published in final edited form as: Sci Transl Med. 2020 Nov 11;12(569):eaax0091. doi: 10.1126/scitranslmed.aax0091

Figure 3.

Figure 3.

α-synuclein oligomer/fibril formation is enhanced by AIMP2 in vitro

(A) ThT fluorescence assay of in vitro aggregation for recombinant α-synuclein (50 uM) and/or GST-AIMP2-FLAG (50 uM) (n = 4 per group).

(B) Silver-stained gel image of in vitro incubation samples of α-synuclein (50 uM) and/or GST-AIMP2-FLAG (50 uM).

(C) Representative immunoblots of α-synuclein or AIMP2 for in vitro incubation samples with various combinations.

(D) Ultrastructure of protein aggregates prepared from α-synuclein incubation (7 d) with either GST or GST-AIMP2-FLAG monitored by a TEM.

(E) Localization of AIMP2 and α-synuclein in protein aggregate formed by in vitro coincubation of recombinant AIMP2 and α-synuclein determined by immuno-Gold EM using 10 nm (green arrow) or 20 nm (blue arrow) nanoGold particles conjugated to anti-AIMP2 and anti-α-synuclein antibodies, respectively.

(F) ThT fluorescence assay of in vitro aggregation for recombinant α-synuclein (50 uM) alone or with small amounts of PFF (2.5 uM) or AIMP2 preformed aggregate (2.5 uM) (n = 3 per group).

Quantified data are expressed as mean ± SEM. Statistical significance was determined by ANOVA test with Tukey post-hoc analysis, **p < 0.01, and ***p < 0.001; NS: not significant.