Abstract
Polycomb group (PcG) proteins are epigenetic repressors that are essential for cell differentiation and development. The Pc protein is a key member of the PcG family and a core component of the Polycomb repressive complex PRC1. In Drosophila, the chromodomain of Pc specifically recognizes the gene silencing mark trimethylated lysine 27 of histone H3 generated by the PRC2 complex, thus delivering the PRC1 complex to targeted chromatin sites. The mammalian Pc homologs, however, bind differentially to methylated histone H3. In addition, other mechanisms may also contribute to the chromatin targeting of Pc and its associated complexes. Here we summarize the current knowledge of the Pc chromodomain and discuss its role as a histone methylation reader from a structural point of view. The cross talk between lysine methylation and other posttranslational modifications on histones and other putative nonhistone targets of Pc protein is also discussed. Recent advancement in the chemical probe development against the chromodomain is also reviewed.
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