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

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发布日期：2012-09-20 20:50 文章来源：丁香园
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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

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