Structural basis for specific binding of polycomb chromodomain to histone H3 methylated at Lys 27

Min, J. R., Zhang, Y., Xu, R. M. (August 2003) Structural basis for specific binding of polycomb chromodomain to histone H3 methylated at Lys 27. Genes & Development, 17 (15). pp. 1823-1828. ISSN 0890-9369

URL: http://www.ncbi.nlm.nih.gov/pubmed/12897052
DOI: 10.1101/gad.269603

Abstract

The chromodomain of Drosophila Polycomb protein is essential for maintaining the silencing state of homeotic genes during development. Recent studies suggest that Polycomb mediates the assembly of repressive higher-order chromatin structures in conjunction with the methylation of Lys 27 of histone H3 by a Polycomb group repressor complex. A similar mechanism in heterochromatin assembly is mediated by HP1, a chromodomain protein that binds to histone H3 methylated at Lys 9. To understand the molecular mechanism of the methyl-Lys 27 histone code recognition, we have determined a 1.4-Angstrom-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide tri-methylated at Lys 27. The structure reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3. The structure also reveals a dPC dimer in the crystal lattice that is mediated by residues specifically conserved in the Polycomb family of chromodomains. The dimerization of dPC can effectively account for the histone-binding specificity and provides new mechanistic insights into the function of Polycomb. We propose that self-association is functionally important for Polycomb.

Item Type: Paper
Uncontrolled Keywords: chromatin histone code histone methylation polycomb chromodomain HETEROCHROMATIN-ASSOCIATED PROTEIN METHYLTRANSFERASE ACTIVITY DROSOPHILA-MELANOGASTER LYSINE-27 METHYLATION X-INACTIVATION DOMAIN HP1 RECOGNITION ASSOCIATION CHROMOSOME
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > Chromatin dynamics
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 > protein structure, function, modification > protein methylation
CSHL Authors:
Communities: CSHL labs > Xu lab
Depositing User: Matt Covey
Date: August 2003
Date Deposited: 02 Apr 2013 16:22
Last Modified: 02 Apr 2013 16:22
PMCID: PMC196225
Related URLs:
URI: http://repository.cshl.edu/id/eprint/27967

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