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. 2021 Jan 19;14:8. doi: 10.1186/s13072-021-00382-y

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 5 — Mass spectrometry analysis of TAP-tag purified Rbm10. a Cells carrying FLAG-HA tagged Rbm10 under its own promoter expressed from its endogenous locus display no detectable silencing defect. Serial dilutions of indicated cells harboring ura4⁺ at the otr region were plated in the EMM medium containing FOA. Ctrl, a control plate without FOA. b A silver-stained gel showing the TAP-tag purification of Rbm10 and a control purification from an untagged strain. c Venn diagram showing the overlap of proteins detected by mass spectrometry. d The proteins identified by mass spectrometry were grouped based on their functions, as indicated in the table