Supplementary information
From the following article:
ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
Xiaobing Shi, Tao Hong, Kay L. Walter, Mark Ewalt, Eriko Michishita, Tiffany Hung, Dylan Carney, Pedro Peña, Fei Lan, Mohan R. Kaadige, Nicolas Lacoste, Christelle Cayrou, Foteini Davrazou, Anjanabha Saha, Bradley R. Cairns, Donald E. Ayer, Tatiana G. Kutateladze, Yang Shi, Jacques Côté, Katrin F. Chua & Or Gozani
Nature 442, 96-99(6 July 2006)
doi:10.1038/nature04835
Supplementary Notes
This file contains the Supplementary Methods, Supplementary Figure Legends and additional references. (1). Nature14097-S1
Supplementary Figure 1
ING2 PHD domain specifically binds in vitro to trimethylated Lysine 4 of histone H3.
Supplementary Figure 2
The ING2 PHD domain D230A mutation specifically abrogates methylated H3K4 binding but not PtdIns(5)P-binding.
Supplementary Figure 3
ING2(PHD) association with H3 is correlated with K4 methylation level in vitro.
Supplementary Figure 4
Methyl-lysine recognition is a property of at least a subset of PHD domains.
Supplementary Figure 5
Silver-stained gels of affinity-purified wild-type and mutant ING2 macromolecular complexes.
Supplementary Figure 6
ING2 occupancy across the cyclin D1 gene correlates with the presence of methylated-H3K4.
Supplementary Figure 7
DNA damage-dependent increased ING2 occupancy at the c-Myc promoter requires H3- triMeK4-binding activity.
Supplementary Figure 8
Model of acute transcriptional repression mediated by ING2 recognition of trimethylated H3K4.
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