[Brainlife] Shi Xiaobing et al (2006) - ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Etiology and Pathogenesis > Tumor Suppressor Genes

Nature, Advance online publication 21 May 2006; doi:10.1038/nature04835

Supplemental Items
	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 and Or Gozani


Notes
	Supplementary Notes This file contains the Supplementary Methods, Supplementary Figure Legends and additional references Notes

Figures
	Supplementary Figure 1 ING2 PHD domain specifically binds in vitro to trimethylated Lysine 4 of histone H3 Fig.1
	Supplementary Figure 2 The ING2 PHD domain D230A mutation specifically abrogates methylated H3K4 binding but not PtdIns(5)P-binding Fig.2
	Supplementary Figure 3 ING2_(PHD) association with H3 is correlated with K4 methylation level in vitro Fig.3
	Supplementary Figure 4 Methyl-lysine recognition is a property of at least a subset of PHD domains Fig.4
	Supplementary Figure 5 Silver-stained gels of affinity-purified wild-type and mutant ING2 macromolecular complexes Fig.5
	Supplementary Figure 6 ING2 occupancy across the cyclin D1 gene correlates with the presence of methylated-H3K4 Fig.6
	Supplementary Figure 7 DNA damage-dependent increased ING2 occupancy at the c-Myc promoter requires H3- triMeK4-binding activity Fig.7
	Supplementary Figure 8 Model of acute transcriptional repression mediated by ING2 recognition of trimethylated H3K4 Fig.8

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