Fig. 1: Demethylation and recognition of Nε-methylated lysines by erasing enzymes and reader proteins. | Communications Chemistry

Fig. 1: Demethylation and recognition of Nε-methylated lysines by erasing enzymes and reader proteins.

From: Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins

Fig. 1

a JmjC KDMs catalyse demethylation of Nε-trimethyllysine residues. Our work explored recognition of the simplest positively charged Nε-trimethyllysine analogue, i.e., the trimethylphosphonium derivative, by Nε-methyllysine binding proteins and Nε-methyllysine demethylases. n: number of methyl groups (3–1). b View from a structure of a JmjC KDM (KDM4AJmjC, light blue) complexed with H3K9me3 (yellow) and NOG (N-oxalylglycine, a 2OG analogue, white) (PDB: 2OQ6). c View from a structure of a reader (TAF3PHD, purple) complexed with H3K4me3 (yellow) (PDB: 2K17). Nitrogen: dark blue; oxygen: red; sulphur: yellow; zinc: grey; nickel: orange.

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