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Title | Menin "reads" H3K79me2 mark in a nucleosomal context. |
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Journal, issue, pages | Science, Vol. 379, Issue 6633, Page 717-723, Year 2023 |
Publish date | Feb 17, 2023 |
Authors | Jianwei Lin / Yiping Wu / Gaofei Tian / Daqi Yu / Eunjeong Yang / Wai Hei Lam / Zheng Liu / Yihang Jing / Shangyu Dang / Xiucong Bao / Jason Wing Hon Wong / Yuanliang Zhai / Xiang David Li / |
PubMed Abstract | Methylation of histone H3 lysine-79 (H3K79) is an epigenetic mark for gene regulation in development, cellular differentiation, and disease progression. However, how this histone mark is translated ...Methylation of histone H3 lysine-79 (H3K79) is an epigenetic mark for gene regulation in development, cellular differentiation, and disease progression. However, how this histone mark is translated into downstream effects remains poorly understood owing to a lack of knowledge about its readers. We developed a nucleosome-based photoaffinity probe to capture proteins that recognize H3K79 dimethylation (H3K79me2) in a nucleosomal context. In combination with a quantitative proteomics approach, this probe identified menin as a H3K79me2 reader. A cryo-electron microscopy structure of menin bound to an H3K79me2 nucleosome revealed that menin engages with the nucleosome using its fingers and palm domains and recognizes the methylation mark through a π-cation interaction. In cells, menin is selectively associated with H3K79me2 on chromatin, particularly in gene bodies. |
External links | Science / PubMed:36795828 |
Methods | EM (single particle) |
Resolution | 3.2 Å |
Structure data | EMDB-34195, PDB-8gpn: |
Source |
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Keywords | GENE REGULATION / Specific histone modification reader |