EED is a crucial component of the Polycomb Repressive Complex 2 (PRC2), which also includes the catalytic subunit EZH2 (Enhancer of zeste 2) and SUZ12 (Suppressor of zeste 12). The PRC2 complex is responsible for the trimethylation of lysine 27 on histone H3 (H3K27me3), a key epigenetic mark associated with transcriptional repression . This modification leads to the repression of target genes, playing a significant role in the regulation of gene expression during development .
EED itself does not possess methyltransferase activity but is essential for the binding of PRC2 to repressive histone marks. This binding is necessary for the propagation of the repressive histone marks and the maintenance of gene silencing .
During embryonic development, the ectoderm is one of the three primary germ layers that form in the early embryo. The ectoderm gives rise to the nervous system, skin, and sensory organs . The role of EED in the PRC2 complex is critical for the proper development of these structures, as it ensures the correct genes are repressed at the right times.
Human recombinant EED is a purified form of the EED protein produced using recombinant DNA technology. This involves inserting the EED gene into a suitable expression system, such as baculovirus-infected insect cells, to produce the protein in large quantities . The recombinant protein is then purified to a high degree of purity (≥95%) for use in research and other applications .
Mutations in the EED gene have been associated with several developmental disorders, including Cohen-Gibson Syndrome and Weaver Syndrome . Understanding the function of EED and its role in the PRC2 complex can provide insights into the molecular basis of these conditions and potentially lead to the development of targeted therapies.