1. Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex
- Author
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Ali Shilatifard, Yoh Hei Takahashi, Hongli Hu, Yidai Yang, Joseph S. Brunzelle, Qianhui Qu, Jean-François Couture, Yan Zhang, and Georgios Skiniotis
- Subjects
0301 basic medicine ,Insecta ,Saccharomyces cerevisiae Proteins ,Methyltransferase ,Stereochemistry ,Lysine ,Saccharomyces cerevisiae ,Chaetomium ,Methylation ,Article ,General Biochemistry, Genetics and Molecular Biology ,Epigenesis, Genetic ,Fungal Proteins ,Histones ,03 medical and health sciences ,Catalytic Domain ,Compass ,Animals ,Humans ,Structural organization ,biology ,Methyltransferase complex ,Cryoelectron Microscopy ,Intracellular Signaling Peptides and Proteins ,Histone-Lysine N-Methyltransferase ,Chromatin ,Yeast ,DNA-Binding Proteins ,Protein Subunits ,030104 developmental biology ,Histone ,Histone Methyltransferases ,biology.protein ,Software - Abstract
The methylation of histone 3 lysine 4 (H3K4) is carried out by an evolutionarily conserved family of methyltransferases referred to as complex of proteins associated with Set1 (COMPASS). The activity of the catalytic SET domain (su(var)3-9, enhancer-of-zeste, and trithorax) is endowed through forming a complex with a set of core proteins that are widely shared from yeast to humans. We obtained cryo-electron microscopy (cryo-EM) maps of the yeast Set1/COMPASS core complex at overall 4.0- to 4.4-Å resolution, providing insights into its structural organization and conformational dynamics. The Cps50 C-terminal tail weaves within the complex to provide a central scaffold for assembly. The SET domain, snugly positioned at the junction of the Y-shaped complex, is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3). The mobile SET-I motif of the SET domain is engaged by Cps30, explaining its key role in COMPASS catalytic activity toward higher H3K4 methylation states.
- Published
- 2018
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