Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex

Zegerman, P., Canas, B., Pappin, D., Kouzarides, T. (April 2002) Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J Biol Chem, 277 (14). pp. 11621-4. ISSN 0021-9258 (Print)0021-9258 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/11850414
DOI: 10.1074/jbc.C200045200

Abstract

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.

Item Type: Paper
Uncontrolled Keywords: Acetylation Blotting, Western Cell Nucleus/metabolism Electrophoresis, Polyacrylamide Gel HeLa Cells Histone Deacetylases/ chemistry/ metabolism Histones/ chemistry/ metabolism Humans Lysine/ chemistry Mass Spectrometry Methylation Mi-2 Nucleosome Remodeling and Deacetylase Complex Peptides/chemistry Precipitin Tests Protein Binding Protein Structure, Tertiary Transcription, Genetic
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation > histone methylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > nucleosome
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > post-translational modification
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Matt Covey
Date: 5 April 2002
Date Deposited: 17 Sep 2014 16:53
Last Modified: 17 Sep 2014 16:53
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30756

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