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. 2023 Apr 10;30(5):594–599. doi: 10.1038/s41594-023-00947-3

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© The Author(s) 2023

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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Extended Data Fig. 10 — (a) Schematic depiction of two-step purification of Domain II mimics followed by mass-spectrometry analysis. Purification of the mimics has been performed similarly to purification of Noc1 RNP except endogenous Cic1 has been C-terminally tagged with streptavidin-biding peptide (sbp). Following purification, samples were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and obtained data normalized using label-free quantification. (b) SDS-PAGE analysis of purified Domain II rRNA mimics. (c) Changes in mean protein abundance, expressed as LFQ values, between purified rRNA mimics: Domain II, 5.8S mutant disrupting helix 2, and rescue mutant restoring helix formation. Error bars represent SD of 3 replicates. (d, e) Structure of Noc1-Noc2 RNP colored accordingly to log2 fold change in protein abundance between (d) 5.8S mutant and Domain II and (e) rescue mutant and 5.8S mutant. Proteins are depicted as cartoons and rRNA as white surface. Helix 2 (H2) is shown in magenta.