Review
doi: 10.1016/j.cbpa.2007.09.011.
Epub 2007 Nov 7.
Modular paths to 'decoding' and 'wiping' histone lysine methylation
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- PMID: 17988933
- DOI: 10.1016/j.cbpa.2007.09.011
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Review
Modular paths to 'decoding' and 'wiping' histone lysine methylation
Curr Opin Chem Biol.
2007 Dec.
Abstract
Specific cell activity results from developmental and environmental control over the expression of our genes. A key component in epigenetic forms of biological regulation is the methylation of lysine residues in histone proteins. This post-translational modification of chromatin has been vigorously studied over the past few years. Highly specific enzymes catalyzing the synthesis and targeted removal of methyl marks, as well as protein motifs recognizing distinct methylated lysines, have been identified. Here, we provide a molecular overview of discrete structural mechanisms that allow these modular proteins to effect and recognize particular lysine methylation imprints on the chromatin polymer.
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