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. 2019 Apr 15;10:1751. doi: 10.1038/s41467-019-09756-z

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© The Author(s) 2019

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 — RNF168^RING binds to the acidic patch of H2A/H2B dimers. a Domain architecture of RNF168: the RING domain is required for ubiquitination, the UDM1 domain mediates recruitment to the DNA damage site through interaction with ubiquitinated H1 and the UDM2 domain binds ubiquitinated H2A-K15. b Sections of the 2D ¹H-¹⁵N correlation spectra of H2A (left) and H2B (right) within the H2A-H2B dimer with increasing amounts of RNF168^RING added. Color coding indicated, the number refers to molar equivalents RNF168 added compared to H2A/H2B dimer. Residues strongly affected by RNF168 binding are labeled in bold. c Normalized peak intensity ratios for H2A (top) and H2B (bottom) upon addition of sub-stoichiometric amounts of RNF168^RING (indicated in Figure in molar equivalents compared to H2A/H2B dimer). Residues with intensities that are one (two) standard deviation (SD) lower than the one-sided 10% trimmed mean are color coded in yellow (red) and labeled. d Residues with significant intensity/chemical shift changes (shown as sticks) cluster predominantly in and around the H2A-H2B acidic patch (see electrostatic view on the right), with additional effects observed for the regions otherwise occluded in the context of the nucleosome (indicated in orange, blue and red). H2B residue labels in italic. Residues in light/dark grey have no significant changes/no data available. e Addition of RNF168^RING results in clear exchange-induced line broadening for H2B residues in and around the acidic patch (V45, L103, T116) but not for residues in non-specific binding regions (I51) as evidenced by ¹⁵N CPMG relaxation dispersion. Color coding indicated in the figure. Best-fits (solid lines) for the acidic patch cluster are consistent with low micromolar dissociation constants and >1 ppm chemical shift changes. Error bars are s.d. based on noise levels in panel (c) and based on three replicate data points in panel (e). Source data are provided as a Source Data file

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