Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2

By P. Peña, F. Davrazou, Xiaobing Shi, Kay L. Walter, V. Verkhusha, O. Gozani, R. Zhao, Tatiana G. Kutateladze. Nature, 2006

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Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4. (2007, methodology): “The TAF3-PHD Finger Directly Binds to Trimethylated Histone H3 Lysine 4 Several papers described interactions between PHD fingers containing proteins (including BPTF) and methylated H3K4 or H3K36 peptides (Li et al., 2006; Pena et al., 2006; Shi et al., 2006; Wysocka et al., 2006).”
Dido3 PHD modulates cell differentiation and division. (2013, neutral): “A similar reduction of binding to H3K4me3 was observed when the corresponding Asp and Glu residues in the ING2 PHD finger were mutated (Peña et al., 2006) (Figure S3).”
A Unique pH-Dependent Recognition of Methylated Histone H3K4 by PPS and DIDO. (2017, background): “In the classic PHD finger proteins, such as BPTF and ING2, this residue could be a tyrosine or serine(Li et al., 2006; Peña et al., 2006), but it is a histidine (H919) in PPS.”
Homeodomain proteins: an update (2015, background): “Further, the PHD finger is a well-characterized zinc finger resembling a RING domain and also plays a role in binding to methylated histones (Pena et al. 2006).”