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Free keywords:
Arginine; binding; chromatin; domains; epigenetic; histone; lysine; methylation; modules
Abstract:
Methylation of histone lysine and arginine residues constitutes a highly complex control system directing
diverse functions of the genome. Owing to their immense signaling potential with distinct sites of
methylation and defined methylation states of mono-, di- or trimethylation as well as their higher
biochemical stability compared with other histone modifications, these marks are thought to be part of
epigenetic regulatory networks. Biological principles of how histone methylation is read and translated
have emerged over the last few years. Only very few methyl marks directly impact chromatin. Conversely,
a large number of histone methylation binding proteins has been identified. These contain specialized
modules that are recruited to chromatin in a methylation site- and state-specific manner. Besides the
molecular mechanisms of interaction, patterns of regulation of the binding proteins are becoming evident.
