title: Affinity purification of MLL3/MLL4 histone H3K4 methyltransferase complex.
abstract: Methylation on histone H3 lysine 4 (H3K4) correlates with actively transcribed genes. In mammalian cells, there exist multiple Set1-like histone H3K4 methyltransferase complexes, which have overlapping but distinct subunit compositions. Developing methods to isolate each of these histone H3K4 methyltransferase complexes would help understand the molecular mechanisms by which histone H3K4 methylation regulates mammalian gene expression. In this chapter, we provide a one-step affinity purification protocol on isolation of the MLL3/MLL4 histone H3K4 methyltransferase complex using FLAG-tagged PA1, a unique subunit of the MLL3/MLL4 complex.
authors: Nuclear Receptor Biology Section, NIDDK, NIH, Bethesda, MD, USA.
authors: Young-Wook
authors: YW
authors: Cho
authors: Sunhwa
authors: S
authors: Hong
authors: Kai
authors: K
authors: Ge
mesh_terms: D004268:DNA-Binding Proteins / Q000378:metabolism*; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000302:isolation & purification* / Q000378:metabolism*; D006801:Humans; D047468:Immunoprecipitation
chemical_list: D004268:DNA-Binding Proteins; C452979:KMT2C protein, human; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; C530816:MLL4 protein, human