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. 2021 Aug 7;49(15):8961–8973. doi: 10.1093/nar/gkab670

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 7. — Modification crosstalk and hierarchical switch of H3-PHF14_PZP engagement. (A,B) ITC fitting curves of H3(1–13)-PHF14_PZP (A) and AF10_PZP (B) titrated with H3_(14–34) peptides with indicated modifications. N.D. = not detected. (C) A model illustrating modification switch features of H3_(1–34)-PHF14_PZP engagement. H3-Nter and H3-middle are colored magenta and orange, respectively. Indicated modifications are shown as color-coded spheres. Strictly sensitive, mildly sensitive, and tolerated modifications are denoted by red cross, half-tick, and tick signs, respectively. (D) A model highlighting hierarchical modification switch features for downregulation of the H3_(1–34)-PHF14_PZP complex formation. H3-Nter and H3-middle are colored magenta and orange, respectively. Hexagonal stars of different colors indicate protein mutations at insertion loop region, mutation at ‘α-ZP’ surface, histone modifications in H3-Nter, and histone modification in H3-middle region, respectively.