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. 2015 Jan 15;29(2):197–211. doi: 10.1101/gad.252189.114

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© 2015 Gong et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 3. — ZMYND8 interacts with chromatin and chromatin-modifying complexes NuRD and BHC. (A) Identification of ZMYND8-interacting factors by MS. Purification scheme of full-length (FL) and PHD–BRD–PWWP-deleted (ΔPBP) SFB-tagged ZMYND8. (SBP) Streptavidin-binding peptide. The table represents ZMYND8 interactors identified in mass spectrum from the indicated experiments. (B) Endogenous ZMYND8 interacts with CHD4, a core component of the NuRD complex. Western blotting analysis of reciprocal co-IPs with the indicated antibodies from HEK293T cells. (C) ZMYND8 MS data. Overlap of full-length (n = 2) and ΔPBP ZMYND8 interactors. (Bottom) Individual interactions based on literature and our MS results. (D–F) The BRD of ZMYND8 interacts with chromatin, and the MYND domain interacts with the NuRD and BHC complexes. (D) Full-length and mutant SFB-ZMYND8 constructs. (E,F) Mapping ZMYND8 interaction domains with interactors. ZMYND8 constructs were transfected into HEK293T and analyzed by co-IP. Full-length and mutant SFB-ZMYND8 were purified using streptavidin beads. (input) Whole-cell extracts. Purified complexes and input were analyzed by Western blotting.