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. 2019 Dec 16;9:19190. doi: 10.1038/s41598-019-55747-x

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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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Aubergine forms homo-oligomers irrespective of its methylation status. (A) Western-blot detection of Aub homo-oligomers resolved with BN-PAGE. Unmethylated and sDMA-Aub (methylated) can form homo-oligomers under native conditions. Aub efficiently oligomerizes at different concentrations in samples shown in different lanes for both unmethylated and methylated Aub. (B) Native size-exclusion chromatography of sDMA-Aub confirms its homo-oligomerization properties. Logarithms of the molecular masses of standard proteins and their corresponding ratios of elution volumes (V_e) and void volume (V_o), measured with the elution volume of blue dextran, were plotted from size-exclusion chromatography experiments (indicated with blue squares). V_e/V_o value of the Aub peak’s central fraction corresponded to the homo-oligomer’s molecular mass of ~500 kDa.