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Unlike the fly PC that recognizes only H3K27Me3, mammalian PC homologues show differential binding to methylated histone.CBX2 and CBX7 bind to both H3K9Me3 and H3K27Me3 whereas CBX4 shows strong affinity for H3K9Me3 [].Significance in Pc G system is apparent from the observation that these genes are not only conserved from plants to animals, but also highly evolved animals have more homologues of Pc G genes.For example, while insects have only one copy of PC, vertebrates have at least five homologues.This complex process is accompanied by differential packaging of the genome in a cell and tissue specific manner that involves post-translational modifications, like methylation and acetylation of histones, and subsequent interaction of other regulatory proteins.

We report the presence of a DNA interaction motif adjacent to chromodomain in all vertebrate PC homologues and suggest a three-way 'PC-histone H3-DNA' interaction that can restrict nucleosome dynamics.

Chromodomain is a three beta strands and a helix containing domain present in proteins that are involved in chromatin organization, viz., HP1, SU(var)3-9, Swi6, CHD1, MSL-3, MOF, etc.

Chromodomain is involved in targeting the protein to specific regions of chromatin.

In this study, we carried out extensive mining and analysis of PC homologues to understand their evolution and sequence-structure-function relationship in the context of motif organization. We used these features to mine PC homologues in the protein sequence database and genome sequence of different organisms and identified 100 PC homologues (Figure ).

Barring the two known domains, PC homologues have not been shown to contain any other distinguishable molecular or structural features.

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