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J. Biol. Chem., Vol. 277, Issue 14, 11621-11624, April 5, 2002
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,
¶
From the 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 (nucleosome
remodeling and deacetylase) binds to the
histone H3 N-terminal tail and that methylation at lysine 4, but not
lysine 9, prevents binding. Given that lysine 4 methylation is found at
sites of active transcription, these results suggest that a function of
lysine 4 methylation is to disrupt the association of histones with a
repressor complex.
Wellcome/Cancer Research
UK Institute, Tennis Court Rd., Cambridge CB2 1QR and the
§ MRC Chemical Research Centre, Hammersmith Hospital,
Du Cane Road, London W12 0NN, United Kingdom
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