Regulation of MLL1 H3K4 methyltransferase activity by its core components

By Y. Dou, T. Milne, Alexander J. Ruthenburg, Seunghee Lee, Jae W. Lee, G. Verdine, C. D. Allis, R. Roeder. Nature Structural &Molecular Biology, 2006

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Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. (2007, methodology): “The control siRNA-treated cells were compared to cells treated with siRNA targeted against CHD1 and ASH2.”
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact (2012, positive): “In addition, purified KMT2A (also known as MLL1) catalyzes the methylation of H3K4 to H3K4me2 (Milne et al., 2002; Nakamura et al., 2002); however, when associated with its endogenous interacting proteins, KMT2A can trimethylate H3K4 (Dou et al., 2006; Schneider et al., 2005).”
Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4. (2007, methodology): “Antibodies specific for H3, H3K4me1, H3K4me2, H3K4me3, and H4 (ab1791, ab8895, ab7766, ab8580, and ab31827) were obtained from Abcam.”
Covalent histone modifications: miswritten, misinterpreted, and miserased in human cancers (2010, background): “MLL forms a large macromolecular nuclear complex with the core complex components (WDR5, RBBP5 and ASL2) and induces H3K4me3 for efficient transcriptio”