6JM9
cryo-EM structure of DOT1L bound to unmodified nucleosome
Summary for 6JM9
| Entry DOI | 10.2210/pdb6jm9/pdb |
| EMDB information | 9843 9844 |
| Descriptor | DNA strand I, DNA strand J, Histone H3.2, ... (8 entities in total) |
| Functional Keywords | histone, nucleosome, methylation, gene regulation |
| Biological source | synthetic construct More |
| Total number of polymer chains | 11 |
| Total formula weight | 201592.86 |
| Authors | Jang, S.,Song, J.J. (deposition date: 2019-03-07, release date: 2019-05-15, Last modification date: 2024-03-27) |
| Primary citation | Jang, S.,Kang, C.,Yang, H.S.,Jung, T.,Hebert, H.,Chung, K.Y.,Kim, S.J.,Hohng, S.,Song, J.J. Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase. Genes Dev., 33:620-625, 2019 Cited by PubMed Abstract: DOT1L is a histone H3 Lys79 methyltransferase whose activity is stimulated by histone H2B Lys120 ubiquitination, suggesting cross-talk between histone H3 methylation and H2B ubiquitination. Here, we present cryo-EM structures of DOT1L complexes with unmodified or H2B ubiquitinated nucleosomes, showing that DOT1L recognizes H2B ubiquitin and the H2A/H2B acidic patch through a C-terminal hydrophobic helix and an arginine anchor in DOT1L, respectively. Furthermore, the structures combined with single-molecule FRET experiments show that H2B ubiquitination enhances a noncatalytic function of the DOT1L-destabilizing nucleosome. These results establish the molecular basis of the cross-talk between H2B ubiquitination and H3 Lys79 methylation as well as nucleosome destabilization by DOT1L. PubMed: 30923167DOI: 10.1101/gad.323790.118 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.3 Å) |
Structure validation
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