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Histone tails undergo methylation at their lysines and arginines. These chemical marks act as traffic signals that direct activity of chromatin remodeling complexes to appropriate regions of the genome. A surprisingly diverse group of effector protein modules in chromatin remodeling complexes and their associated factors are involved in the recognition of histone methyllysines. Previous studies generally painted a picture of individual lysines recognized by these protein modules in a 1:1 fashion. However, recent structural studies show more complex interactions where the critical lysines are recognized in pairs, or in the context of nucleosomal DNA, or within the central pore of repeat motifs. These interactions extend our understanding of how histone tail recognition can be enhanced through coupled interactions within a single module or through the cooperation of two different molecules.

Original publication

DOI

10.1016/j.sbi.2011.10.001

Type

Journal article

Journal

Curr Opin Struct Biol

Publication Date

12/2011

Volume

21

Pages

744 - 749

Keywords

Animals, Chromatin, DNA, Histones, Humans, Lysine, Methylation, Models, Molecular, Nucleosomes, Protein Conformation