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Title | Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex. |
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Journal, issue, pages | Cell, Vol. 174, Issue 5, Page 1117-1126.e12, Year 2018 |
Publish date | Aug 23, 2018 |
Authors | Qianhui Qu / Yoh-Hei Takahashi / Yidai Yang / Hongli Hu / Yan Zhang / Joseph S Brunzelle / Jean-Francois Couture / Ali Shilatifard / Georgios Skiniotis / |
PubMed 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 ...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. |
External links | Cell / PubMed:30100186 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.818 - 4.3 Å |
Structure data | EMDB-7303, PDB-6bx3: PDB-6e29: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | GENE REGULATION/Transferase / Histone H3K4 Methyltransferase / GENE REGULATION-Transferase complex / PROTEIN BINDING / histone / epigenetics / COMPASS / histone H3 Lys-4 methylation / MLL1 / SET1 |