Histone N-terminal tails are post-translationally modified in many ways. At lysine residues,
histones can be either acetylated or methylated. Both modifications lead to the binding of
specific proteins; bromodomain proteins, such as GCN5, bind acetyl lysines and the
chromodomain protein, HP1, binds methyl lysine 9 of histone H3. Here we show that the
previously characterized transcriptional repressor complex NuRD (nucleosomeremodeling
and deacetylase) binds to the histone H3 N-terminal tail and that methylation at lysine 4, but …