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. 2019 Dec 12;9:18983. doi: 10.1038/s41598-019-55528-6

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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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Amyloid aggregation of FXR1 protein depends on its N-terminal region. (a) The FXR1N(1-379)-YFP protein forms visible aggregates in yeast cells, whereas FXR1C(380-568)-YFP is evenly distributed in cytoplasm. Scale bar, 10 µm. Three independently obtained transformants expressing the FXR1N(1-379)-YFP and FXR1C(380-568)-YFP proteins were included in the analysis. About one hundred cells of each transformant were analyzed. (b) Protein lysates expressing the FXR1N(1-379)-YFP and FXR1C(380-568)-YFP proteins were centrifuged, separated into the soluble and insoluble fractions and analyzed by immunoblotting. The FXR1N(1-379)-YFP protein forms insoluble aggregates, whereas the FXR1C(380-568)-YFP is present in soluble form. P – pellet fraction; S - supernatant fraction. (c,d) - Relative intensities of bands corresponding to monomers and aggregates of FXR1N(1-379)-YFP and FXR1C(380-568)-YFP represented as mean ± SEM, for three independent protein samples.