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. 2019 Sep 23;47(19):10426–10438. doi: 10.1093/nar/gkz819

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© The Author(s) 2019. 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 License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 7. — The model for the role of RBBP5_CTD in regulating MLL1 complex. The interaction between RBBP5_WD40 and RBBP5_CTD facilitates the formation of a compact MLL1 complex with correct coordination of the structural elements required for methylation. The loss of RBBP5_CTD generates an extended complex with low catalytic efficiency. A vertebrate-specific RBBP5_CTD3 can bind to nucleosome DNA and increases the association of the MLL1 complex with nucleosomes, thereby promoting methylation of nucleosomal H3.