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. 2013 Mar 15;27(6):596–601. doi: 10.1101/gad.211425.112

Figure 3.

Figure 3.

The AS1–AS2 complex physically interacts with PRC2 and directly recruits this complex to BP and KNAT2. (A) ChIP analyses showing CLF occupancy at specific regions of BP and KNAT2. CLF occupancy at these sites is significantly reduced in as1 compared with wild type. (*) P < 0.05; (**) P < 0.01. Values (mean ± SE; n ≥ 3) are relative to the enrichment of CLF at AG. (B) In plants carrying an inducible AS2-YFP fusion (pOlexA:AS2-YFP), MYC-CLF (top panel) and FIE-HA (bottom panel) coimmunoprecipitate with AS2-YFP specifically upon induction. AS2-YFP also coimmunoprecipitates with MYC-CLF (top panel) and FIE-HA (bottom panel) in immunoprecipitation assays with anti-MYC and anti-HA antibody, respectively, but not in control immunoprecipitation assays with IgG. Antibodies used in immunoprecipitation assays are listed at the top, and proteins detected by Western are at the right. (C) Bimolecular fluorescence complementation assays reveal direct physical interactions between AS1 and the PRC2 core components FIE and CLF and between AS2 and EMF2. Cobombardment of functional AS2 and CLF fusion constructs (Supplemental Table 2) yields no fluorescence signal. (Left panels) EYFP signal monitoring protein–protein interactions. (Middle panels) DAPI staining indicating positions of nuclei. (Right panels) Merged images.