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-Structure paper
| タイトル | Trypanosome histone variants H3.V and H4.V promote nucleosome plasticity in repressed chromatin. |
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| ジャーナル・号・ページ | Structure, Vol. 34, Issue 4, Page 629-644.e10, Year 2026 |
| 掲載日 | 2026年4月2日 |
著者 | Gauri Deák / Hayden Burdett / James A Watson / Marcus D Wilson / ![]() |
| PubMed 要旨 | Histone variants define distinct chromatin states by modulating the biophysical properties of nucleosomes. Variants play a particularly important role in the parasitic protist Trypanosoma brucei, ...Histone variants define distinct chromatin states by modulating the biophysical properties of nucleosomes. Variants play a particularly important role in the parasitic protist Trypanosoma brucei, which has unusual chromatin and lacks a canonical repressive heterochromatin system. Instead, T. brucei utilizes specialized divergent histone variants H3.V and H4.V. However, the biochemical basis of their repressive functions is unknown. Here, we determined the structure of the H3.V-H4.V nucleosome core particle and biochemically characterized variant-containing nucleosomes and nucleosome arrays, probing their unique properties. We discovered that surprisingly for repressive-state nucleosomes, H3.V promotes pronounced DNA splaying, largely via its N-terminal tail region, while retaining overall stability that is comparable to canonical nucleosomes. In contrast, H4.V exhibits near-identical binding to DNA but mediates a slight increase in histone octamer stability. The surface of the H3.V-H4.V nucleosome is altered and provides a differential platform for chromatin-binding proteins, linking the variants to parasite pathogenicity. |
リンク | Structure / PubMed:41709455 |
| 手法 | EM (単粒子) |
| 解像度 | 3.21 - 3.99 Å |
| 構造データ | EMDB-53505, PDB-9r1d: ![]() EMDB-55943: Structure of the H4.V variant nucleosome core particle from Trypanosoma brucei |
| 由来 |
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キーワード | DNA BINDING PROTEIN / nucleosome / histone / nucleus |
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