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

Abstract

N ε-methylation of lysine residues in histones plays an essential role in the regulation of eukaryotic transcription, and understanding the extent to which histone N ε-methyllysine readers and erasers can manifest selectivity is of fundamental and medicinal interest. Here, the authors study the phosphonium analogue of N ε-trimethyllysine, finding that a subtle substitution from nitrogen to phosphorus substantially affects its interactions with N ε-methyllysine readers and erasers.