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. 2017 Jul 19;7:5853. doi: 10.1038/s41598-017-05829-5

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© The Author(s) 2017

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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The N terminal region of Sup35 crosslinks to Rnq1. Site-directed crosslinking of Sup35-G7C to Rnq1 created high-molecular weight aggregates as visualized by SDD-AGE. Rnq1 alone, Sup35-G7C alone, and both proteins together without SMPB did not create large aggregates. The “⁺*” notation in the fifth lane indicates Sup35 monomer following treatment with TCEP. Western blot is a representative image from three independent experiments. In the lower blot, Rnq1 loading was confirmed by SDS-PAGE. Vertical white bars separate non-adjacent lanes of the same blot. The dashed line separates adjacent lanes of the same blot under differing film exposures for image clarity (full blots in Supplementary Figure S4). There is excess Rnq1 in lanes 1 and 3, samples prepared without crosslinker, to adjust for protein that is lost during sample desalting following attachment of the crosslinker (see Methods). Three trials of crosslinking were included in each experiment and the crosslinking experiment was repeated with different batches of purified proteins three times.