H3K27me3 modified histone binding

Definition

Target type: molecularfunction

Binding to a histone H3 in which the lysine residue at position 27 has been modified by trimethylation. [GOC:dph, PMID:23948251]

H3K27me3, a histone modification characterized by the trimethylation of lysine 27 on histone H3, serves as a critical epigenetic mark associated with gene silencing. The molecular function of H3K27me3 modified histone binding involves the recognition and interaction of specific proteins, known as 'readers,' with the trimethylated lysine residue. These readers possess specialized domains, such as the Polycomb repressive complex 1 (PRC1) chromodomain, which exhibit high affinity for H3K27me3. Upon binding, the reader proteins act as molecular scaffolds, recruiting additional proteins and enzymatic complexes to the chromatin region marked by H3K27me3. This recruitment leads to the formation of large protein complexes that consolidate gene repression. For instance, PRC1, which contains H3K27me3 readers, contributes to the compaction of chromatin structure, inhibiting access of transcription factors and RNA polymerase II to the DNA. Furthermore, other reader proteins may possess enzymatic activity, such as histone methyltransferases, which further reinforce H3K27me3 deposition and maintain gene silencing. The interplay between H3K27me3 readers, associated proteins, and chromatin modifications ultimately shapes the epigenetic landscape, playing a crucial role in regulating gene expression during development, differentiation, and disease states.'
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Proteins (1)

Compounds (3)