|Title||Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase.|
|Journal, issue, pages||Genes Dev., Vol. 33, Issue 11-12, Page 620-625, Year 2019|
|Publish date||Jun 1, 2019|
|Authors||Seongmin Jang / Chanshin Kang / Han-Sol Yang / Taeyang Jung / Hans Hebert / Ka Young Chung / Seung Joong Kim / Sungchul Hohng / Ji-Joon Song /|
|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 ...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.|
|External links||PubMed:30923167 / Publisher's page|
|Keywords||Arginine / Catalytic Domain / Cryoelectron Microscopy / DOT1L protein, human / Histone-Lysine N-Methyltransferase / Histones / Humans / Hydrophobic and Hydrophilic Interactions / Methylation / Methyltransferases / Models, Molecular / Nucleosomes / Protein Stability / Protein Structure, Secondary / Ubiquitin / Ubiquitination / GENE REGULATION / histone / nucleosome|
|Methods||EM (single particle)|
|Resolution||6.8 - 7.3 A|
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