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. 2020 Feb 10;11:809. doi: 10.1038/s41467-020-14595-4

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© The Author(s) 2020

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 HU sensitivity was determined with H3 (WT), H3K4A, H3R2A, H3K36A and H3K79A mutations in the RAD53 or rad53-K227A backgrounds. b Immunoblot showing H3K4me1/2/3 levels in set1Δ bre2Δ and spp1Δ strains. c HU sensitivity was determined with WT, set1Δ, bre2Δ, and spp1Δ in the RAD53 or rad53-K227A backgrounds. d Cell viability after G1 synchronization and release into 25 mM of HU for the indicated time for H3, H3K4A, set1Δ, bre2Δ and spp1Δ on RAD53 or rad53-K227A backgrounds. Data are the mean ± SD (n = 3 biological replicates). e Immunoblot showing levels of phosphorylated H2AS129 (γH2A) in set1Δ, bre2Δ and spp1Δ on the rad53-K227A background after G1-release in 0 mM (−) or 5 mM HU (+) for the indicated time.