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. Author manuscript; available in PMC: 2011 Apr 12.
Published in final edited form as: Nat Rev Genet. 2010 Mar;11(3):204–220. doi: 10.1038/nrg2719

Figure 3. Model depicting recruitment of the de novo methylation machinery by unmethylated histone 3 lysine 4 (H3K4) tails.

Figure 3

The amino-terminal domain of Dnmt3L possesses a cysteine rich domain that interacts with unmethylated H3K4 tails and this interaction is proposed to recruit or activate Dnmt3a2. The carboxy-terminal domains of Dnmt3L and Dnmt3a form a tetrameric complex in which two Dnmt3a proteins interact with each other and are flanked by two Dnmt3L proteins. The Dnmt3a active sites (red stars) are thought to be separated by approximately one helical turn and thus could catalyze methylation (filled circles) on opposite DNA strands ~10bps apart. Once recruited to a specific locus, the Dnmt3L/Dnmt3a tetramer might be able to oligomerize, which could result in an ~10bp periodic pattern of DNA methylation along the same DNA strand.