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. 2021 Jun 9;12:3497. doi: 10.1038/s41467-021-23636-5

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© The Author(s) 2021

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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Fig. 1 — a Scheme representing the generation of ubiquitylated histones. Aha was incorporated into Ub via selective pressure incorporation and Plk into H1.2 by stop codon suppression. Finally, the proteins were linked by CuAAC. H1.2 was ubiquitylated at positions K17, K64, and K206. b Non-ubiquitylated H1.2 and H1.2 KxUbs resolved by SDS-PAGE followed by Coomassie blue staining. c LC-MS analysis of full-length proteins. H1.2 calc. 23370 Da, measured 23370 Da; H1.2 K17Ub calc. 32813 Da, measured 32818 Da; H1.2 K64Ub calc. 32813 Da, measured 32816 Da; H1.2 K206Ub calc. 32813 Da, measured 32815 Da. d Stability assay of H1.2 and H1.2 KxUbs. Proteins were incubated in HEK 293T cell lysate and analyzed by western blot showing constant levels of the respective proteins, indicating the stability of the conjugates over time at various temperatures.