title: Modular paths to 'decoding' and 'wiping' histone lysine methylation.
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.
authors.affiliation: Gene Expression Unit, Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117, Heidelberg, Germany.
authors.forename: Georg
authors.initials: G
authors.lastname: Kustatscher
authors.forename: Andreas G
authors.initials: AG
authors.lastname: Ladurner
mesh_terms: D000595:Amino Acid Sequence; D002843:Chromatin / Q000378:metabolism*; D044127:Epigenesis, Genetic; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D002843:Chromatin; D006657:Histones; D008239:Lysine