Methyl lysine-binding proteins

Fig. 8. Proposed models that link histone methylation to DNA methylation (for details see Section 5.2). Methylated cytosines attract histone methyltransferases that contain a methyl-binding domain or a methyl-CpG binding protein (MeCP2) that recruits histone methylase activities these introduce methyl groups into the histone tails. The binding of chromodomain HPl proteins to H3 tails methylated at lysine 9 generates a secondary layer of repressive chromatin structure, (b) In a reverse scenario, methylated histone tails attract chromodomain-binding proteins, which in turn recruit Dmnts to methylate adjacent DNA sequences.

Sarraf S.A. and Stancheva, I. (2004) Methyl-CpG binding protein MBDl couples histone H3 methylation at lysine 9 by SETDBl to DNA replication and chromatin assembly. Molecular Cell, 15, 595-605. 

New evidence indicates that the major mediators in remodeler recruitment may be bromo and chromo domain-containing proteins. Bromo domains mediate protein binding to acetyl-lysines in histones and other proteins (Jacobson et al., 2000), and chromo domains have been shown to bind methyl-lysines (Jacobs et al., 2002). For instance, TAF1, a component of TFIID, contains two tandem bromo domains that bind selectively to multiply acetylated H4 peptides (Jacobson et al., 2000). Furthermore, the Gcn5 bromo domain preferentially binds acetylated H4 K16 (Owen et al., 2000). 

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