| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979175 | Current Opinion in Structural Biology | 2011 | 6 Pages |
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.
► Recognition of histone methyllysines by diverse modules is precursor to a variety of epigenetic phenomena. ► The ADD domain associated with the mental retardation syndrome reads the methylation status of lysines 4 and 9 in the histone H3 correlated with gene repression. ► The MSL3 Chromodomain of the MSL dosage compensation complex recruits DNA to bind to the monomethylated lysine 20 in histone H4. ► The WD40 repeats in the PRC2 complex form a 7-blade β-propeller with multiple blades involved in coordination of a trimethylated lysine that signals gene repression.
