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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Connecting the DOTs: covalent histone modifications and the formation of silent chromatin.

Histone methylation has emerged as a significant regulator of chromatin structure and function. Two different classes of histone methyltransferase ( HMT) have been described, which target either lysine or arginine residues in the histone N-terminal tails. A flurry of recent papers now describe a third class of HMT that affects chromatin silencing indirectly, not by methylation of histone tails, but instead by targeting a conserved lysine residue in the core domain of the nucleosome.[1]

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