ArticleLife science alliance2021
Structural basis of nucleosomal histone H4 lysine 20 methylation by SET8 methyltransferase.
Article in Life science alliance, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- APC coordinates GSK3 phosphorylation of SETD8 to suppress colorectal cancer.Cell reports · 2026Article
- AlphaFold-guided structural analyses of nucleosome binding proteins.Nucleic acids research · 2025Article
- Bioluminescence in Clinical and Point-of-Care Testing.Biosensors · 2025Review
- Semisynthesis of Isomerized Histone H4 Reveals Robustness and Vulnerability of Chromatin toward Molecular Aging.Journal of the American Chemical Society · 2025Article
- High-Resolution Cryo-EM Analyses of Nucleosomes.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Epigenetic Regulation of Fungal Secondary Metabolism.Journal of fungi (Basel, Switzerland) · 2024Review
- Structural basis of nucleosomal H4K20 recognition and methylation by SUV420H1 methyltransferase.Cell discovery · 2023Article
- DOT1L regulates chromatin reorganization and gene expression during sperm differentiation.EMBO reports · 2023Article
- The engagement of histone lysine methyltransferases with nucleosomes: structural basis, regulatory mechanisms, and therapeutic implications.Protein & cell · 2023Review
- Oocyte-Specific Knockout of Histone Lysine Demethylase KDM2a Compromises Fertility by Blocking the Development of Follicles and Oocytes.International journal of molecular sciences · 2022Article
- Multivalent DNA and nucleosome acidic patch interactions specify VRK1 mitotic localization and activity.Nucleic acids research · 2022Article
- Structural studies of functional nucleosome complexes with transacting factors.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022Review
- Determination of Histone Methyltransferase Structures in Complex with the Nucleosome by Cryogenic Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Principles of nucleosome recognition by chromatin factors and enzymes.Current opinion in structural biology · 2021Review
- Structural features of nucleosomes in interphase and metaphase chromosomes.Molecular cell · 2021Article
- Is There a Histone Code for Cellular Quiescence?Frontiers in cell and developmental biology · 2021Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SET8 is solely responsible for histone H4 lysine-20 (H4K20) monomethylation, which preferentially occurs in nucleosomal H4. However, the underlying mechanism by which SET8 specifically promotes the H4K20 monomethylation in the nucleosome has not been elucidated. Here, we report the cryo-EM structures of the human SET8-nucleosome complexes with histone H3 and the centromeric H3 variant, CENP-A. Surprisingly, we found that the overall cryo-EM structures of the SET8-nucleosome complexes are substantially different from the previous crystal structure models. In the complexes with H3 and CENP-A nucleosomes, SET8 specifically binds the nucleosomal acidic patch via an arginine anchor, composed of the Arg188 and Arg192 residues. Mutational analyses revealed that the interaction between the SET8 arginine anchor and the nucleosomal acidic patch plays an essential role in the H4K20 monomethylation activity. These results provide the groundwork for understanding the mechanism by which SET8 specifically accomplishes the H4K20 monomethylation in the nucleosome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.