Article body
Histones can be covalently modified by the addition of various chemical appendages, and distinct histone marks are associated with most DNA transactions (transcription, repair, and so on) and have been implicated as carriers of epigenetic identity. However, the precise mechanisms that connect histone marks to functional consequences are only beginning to emerge. Combinations of histone marks appear to regulate the functional �readout� of the chromatin fibre, either directly or via specific protein adaptors termed effectors. Recent research suggests that effector modules bind to histone tails in a modification–specific and methyl–state–specific manner. Emerging hints that putative effector modules coexist within the same protein complex suggest that multivalent engagement of chromatin subunits may be a functionally important phenomenon.
This Poster illustrates well–known histone marks and representative examples of histone–binding effector modules, and outlines emerging themes in the molecular recognition of modified histones. The authors further propose a nomenclature to describe the possible modes of multivalent chromatin mark recognition. The Poster is freely available thanks to support from Abcam.
