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. Author manuscript; available in PMC: 2014 Aug 3.
Published in final edited form as: Nature. 2013 May 1;498(7454):385–389. doi: 10.1038/nature12178

Figure 4. Structural basis for recognition of H3(1–15)K9me2 peptide by the SHH1 SAWADEE domain and the functional impact of mutations of residues lining the K4 and K9me2 pockets.

Figure 4

a, Overall structure of the H3(1–15)K9me2-SAWADEE complex with the SAWADEE domain as a ribbon diagram and the peptide as a stick representation. The simulated annealing composite omit map at 1σ level of the bound peptide is also shown. b, Stereo view highlighting the intermolecular interactions between the SAWADEE domain and the bound peptide. Intermolecular hydrogen-bonding interactions are designated by dashed red lines. c, d and e, Close-up views of H3 lysine residues in their respective binding pockets. f and g, Boxplots of genome-wide % CHH methylation and siRNA levels in wild-type, shh1 mutants, and shh1 mutants transformed with SHH1 constructs (shh1 + SHH1) that encode wild-type SHH1 or K9 (F162AF165A and Y140A) or K4 (D141A and Y212A) binding pocket mutants. h, qPCR of Pol-IV enrichment in the backgrounds described in f at a defined Pol IV binding site. Bars are the average of two biological replicates normalized to input and actin levels (+/− SE).