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Reference Report
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| Citation | Min, J., Zhang, Y., Xu, R.M. (2003). Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 17(15): 1823--1828. (Export to RIS) | ||
| FlyBase ID | FBrf0162134 | ||
| Publication Type | Research paper | ||
| PubMed ID | 12897052 | ||
| PubMed 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-A-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide trimethylated 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. | ||
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| Language of Publication | English | ||
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Parent Publication
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| Publication Type | Journal | ||
| Abbreviation | Genes Dev. | ||
| Title | Genes & Development | ||
| Publication Year | 1987- | ||
| ISBN/ISSN | 0890-9369 | ||
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Data from Reference
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| Genes (3)
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