研究実績
2025
1.
Tomoya Kujirai, Kenta Echigoya, Yusuke Kishi, Mai Saeki, Tomoko Ito, Junko Kato, Lumi Negishi, Hiroshi Kimura, Hiroshi Masumoto, Yoshimasa Takizawa, Yukiko Gotoh, Hitoshi Kurumizaka
Structural insights into how DEK nucleosome binding facilitates H3K27 trimethylation in chromatin Journal Article
In: Nature Structural & Molecular Biology, 2025, ISSN: 1545-9993.
Abstract | Links | タグ: Gotoh G, Kimura G, Kurumizaka G
@article{10.1038/s41594-025-01493-w,
title = {Structural insights into how DEK nucleosome binding facilitates H3K27 trimethylation in chromatin},
author = {Tomoya Kujirai and Kenta Echigoya and Yusuke Kishi and Mai Saeki and Tomoko Ito and Junko Kato and Lumi Negishi and Hiroshi Kimura and Hiroshi Masumoto and Yoshimasa Takizawa and Yukiko Gotoh and Hitoshi Kurumizaka},
doi = {10.1038/s41594-025-01493-w},
issn = {1545-9993},
year = {2025},
date = {2025-02-21},
urldate = {2025-02-21},
journal = {Nature Structural & Molecular Biology},
abstract = {Structural diversity of the nucleosome affects chromatin conformations and regulates eukaryotic genome functions. Here we identify DEK, whose function is unknown, as a nucleosome-binding protein. In embryonic neural progenitor cells, DEK colocalizes with H3 K27 trimethylation (H3K27me3), the facultative heterochromatin mark. DEK stimulates the methyltransferase activity of Polycomb repressive complex 2 (PRC2), which is responsible for H3K27me3 deposition in vitro. Cryo-electron microscopy structures of the DEK–nucleosome complexes reveal that DEK binds the nucleosome by its tripartite DNA-binding mode on the dyad and linker DNAs and interacts with the nucleosomal acidic patch by its newly identified histone-binding region. The DEK–nucleosome interaction mediates linker DNA reorientation and induces chromatin compaction, which may facilitate PRC2 activation. These findings provide mechanistic insights into chromatin structure-mediated gene regulation by DEK.},
keywords = {Gotoh G, Kimura G, Kurumizaka G},
pubstate = {published},
tppubtype = {article}
}
Structural diversity of the nucleosome affects chromatin conformations and regulates eukaryotic genome functions. Here we identify DEK, whose function is unknown, as a nucleosome-binding protein. In embryonic neural progenitor cells, DEK colocalizes with H3 K27 trimethylation (H3K27me3), the facultative heterochromatin mark. DEK stimulates the methyltransferase activity of Polycomb repressive complex 2 (PRC2), which is responsible for H3K27me3 deposition in vitro. Cryo-electron microscopy structures of the DEK–nucleosome complexes reveal that DEK binds the nucleosome by its tripartite DNA-binding mode on the dyad and linker DNAs and interacts with the nucleosomal acidic patch by its newly identified histone-binding region. The DEK–nucleosome interaction mediates linker DNA reorientation and induces chromatin compaction, which may facilitate PRC2 activation. These findings provide mechanistic insights into chromatin structure-mediated gene regulation by DEK.
