Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex.

Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex.
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DOI:
10.1016/j.cell.2018.07.020
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发表时间:
2018-08-23
期刊:
影响因子:
64.5
通讯作者:
Skiniotis G
Skiniotis G
中科院分区:
生物学1区
文献类型:
--
作者:
Qu Q;Takahashi YH;Yang Y;Hu H;Zhang Y;Brunzelle JS;Couture JF;Shilatifard A;Skiniotis G

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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 4.0–4.4 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 towards higher H3K4 methylation states. The cryo-EM structure of the complete yeast COMPASS complex points to how it controls selective H3K4 mono-, di- and tri-methylation. Structure of a COMPASS histone H3K4 methyltransferase complex
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