Fig. 3: Swi6-Y and Swi6-K variants disrupt a direct interaction with Epe1. | Nature Communications

Fig. 3: Swi6-Y and Swi6-K variants disrupt a direct interaction with Epe1.

From: Epigenetic memory is governed by an effector recruitment specificity toggle in Heterochromatin Protein 1

Fig. 3

a X-ray crystallography structure of a Swi6-CSD dimer (PDB 1E0B, 1.90 Å). The dimerization interface and the side chains of Leu 315, a residue crucial for dimerization, are labeled. Thr 278 maps to a beta sheet interface with its side chain facing outward away from the dimerization interface. b Western blots of V5 coimmunoprecipitation (CoIP) performed with cell lysates to test the interaction between Epe1-V5 and Swi6. Epe1 is detected using a V5 antibody and Swi6 is detected using a primary antibody. c, d ChIP-seq of H3K9me2 (c) and H3K9me3 (d) surrounding the ura4Δ::10XtetO-ade6+ reporter in indicated genotypes and tetracycline treatment. The ura4Δ::10XtetO-ade6+ reporter is highlighted in red, displayed in a 40 kb region. Enrichment in all samples is shown as normalized reads per kilobase million (RPKM). Source data are provided as Source Data File.

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