This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.
This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Correction: miR-29a contributes to breast cancer cells epithelial-mesenchymal transition, migration, and invasion via downregulating histone H4K20 trimethylation through directly targeting SUV420H2.
miR-29a contributes to breast cancer cells epithelial-mesenchymal transition, migration, and invasion via down-regulating histone H4K20 trimethylation through directly targeting SUV420H2.
Mapping H4K20me3 onto the chromatin landscape of senescent cells indicates a function in control of cell senescence and tumor suppression through preservation of genetic and epigenetic stability.
miR-29a contributes to breast cancer cells epithelial-mesenchymal transition, migration, and invasion via down-regulating histone H4K20 trimethylation through directly targeting SUV420H2.
SUV420H2 is strongly associated to pericentric heterochromatin, the N-terminus of SUV420H2 comprising then catalytically active SET domain is dispersed within the nucleus, whereas the C-terminal part of the protein is associated with heterochromatin
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the SET domain is composed of three groups of canonical beta-sheets arranged in a triangular fashion with a group of two beta-sheets closely neighboring a conserved alpha-helix defining a cleft for the binding to the histone-tail ligand. The cofactor AdoMet and substrate bind at two adjacent sites to the SET domain. The histone-tail ligand binds into a groove formed by both the SET and postSET domains. The cofactor AdoMet binds into a distinct pocket located on the other side of the SET domain and acts as a methyl group donor. Both AdoMet and the L-lysine-histone are connected through a narrow tunnel where the methyl group is channeled. In the structure of the peptide-less NSDx02SET domain, the postSET domain loop is extended on top of the histone binding site, which sterically prevents the binding of either H3K36 or H4K20 substrates. In the presence of ligand, a network of residues stabilizes the H4-peptide tail on the binding site