Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex

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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. The cryo-EM structure of a fully functional COMPASS complex reveals the intricate structural coordination of the methyltransferase subunit by its partner proteins.

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Qu, Q., Takahashi, Y. hei, Yang, Y., Hu, H., Zhang, Y., Brunzelle, J. S., … Skiniotis, G. (2018). Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex. Cell, 174(5), 1117-1126.e12. https://doi.org/10.1016/j.cell.2018.07.020

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