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. 2020 Mar 6;11:1222. doi: 10.1038/s41467-020-15006-4

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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. 3 — a Reciprocal immunoprecipitation of PAF15 and DNMT1 from chromatin lysates. IP was performed with control (Mock), anti-xDNMT1 (DNMT1), or anti-xPAF15 (PAF15) antibody from chromatin lysates. Supernatants after immunoprecipitation (IP-sup) or immunoprecipitates (IP-ppt) were analyzed by immunoblotting using the indicated antibodies. b Sperm chromatin was replicated in interphase egg extracts containing xPAF15-Flag₃ [wild-type, K18R, K27R, or K18RK27R (KRKR)]. Isolated and solubilized chromatin proteins were subjected to immunoprecipitation using anti-Flag antibodies. The resultant immunoprecipitates were analyzed by immunoblotting using the indicated antibodies. c Superimposition of plots of enthalpy changes in the interaction between hRFTS and hPAF15_2-30 or its ubiquitylated analogs by ITC measurement. d Pull-down of ubiquitylated PAF15 from denatured chromatin extracts using recombinant wild-type xDNMT1-Flag₃ and its ubiquitin-binding mutants (P253AL256A or I317AI362A). Source data are provided as a Source Data file.