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Originally published In Press as doi:10.1074/jbc.C200045200 on February 15, 2002

J. Biol. Chem., Vol. 277, Issue 14, 11621-11624, April 5, 2002
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ACCELERATED PUBLICATION
Histone H3 Lysine 4 Methylation Disrupts Binding of Nucleosome Remodeling and Deacetylase (NuRD) Repressor Complex*

Philip ZegermanDagger , Benito Canas§, Darryl Pappin§, and Tony KouzaridesDagger

From the Dagger  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

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.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. E-mail: tk106@cam.ac.uk.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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