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-Structure paper
| Title | AlphaFold-guided structural analyses of nucleosome binding proteins. |
|---|---|
| Journal, issue, pages | Nucleic Acids Res, Vol. 53, Issue 14, Year 2025 |
| Publish date | Jul 19, 2025 |
Authors | Xin Yang / Haoqiang Zhu / Liuxin Shi / Tingrui Song / Weibin Gong / Shunmin He / Shan Shan / Chunfu Xu / Zheng Zhou / ![]() |
| PubMed Abstract | The nucleosome, as the fundamental unit of chromatin, interacts with a diverse range of proteins, crucially regulating gene expression. In this study, we introduce an AlphaFold-based algorithm ...The nucleosome, as the fundamental unit of chromatin, interacts with a diverse range of proteins, crucially regulating gene expression. In this study, we introduce an AlphaFold-based algorithm designed to analyze nucleosome-binding proteins from a dataset of over 7600 human nuclear proteins. Using proteins that interact with the nucleosome acidic patch as a benchmark, our screening achieves a successful prediction rate of 77% (23 out of 30 proteins). This predictive approach has led to the identification of ARID4A and ARID4B as novel nucleosome-binding proteins. Additionally, this analytical method was used to study RING-family ubiquitin E3 ligase RNF168, demonstrating that RNF168 dimerization enhances its binding to the nucleosome, a finding confirmed by cryogenic-electron microscopy structural analysis. Our findings offer a rapid and effective method for the discovery and characterization of nucleosome-binding proteins and emphasize the significant role of ubiquitin E3 ligase dimerization in epigenetic regulation. |
External links | Nucleic Acids Res / PubMed:40794873 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.9 Å |
| Structure data | EMDB-62494, PDB-9kq2: |
| Chemicals | ![]() ChemComp-ZN: |
| Source |
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Keywords | DNA BINDING PROTEIN/DNA / DNA repair / Histone ubiquitination / Nucleosome / E3 ubiquitin-protein ligase / RNF168 / DNA BINDING PROTEIN-DNA complex |
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