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-Structure paper
| タイトル | Mechanisms of chromatin remodeling by an Snf2-type ATPase. |
|---|---|
| ジャーナル・号・ページ | bioRxiv, Year 2025 |
| 掲載日 | 2025年1月2日 |
著者 | Deepshikha Malik / Ashish Deshmukh / Silvija Bilokapic / Mario Halic / ![]() |
| PubMed 要旨 | Chromatin remodeling enzymes play a crucial role in the organization of chromatin, enabling both stability and plasticity of genome regulation. These enzymes use a Snf2-type ATPase motor to move ...Chromatin remodeling enzymes play a crucial role in the organization of chromatin, enabling both stability and plasticity of genome regulation. These enzymes use a Snf2-type ATPase motor to move nucleosomes, but how they translocate DNA around the histone octamer is unclear. Here we use cryo-EM to visualize the continuous motion of nucleosomal DNA induced by human chromatin remodeler SNF2H, an ISWI family member. Our work reveals conformational changes in SNF2H, DNA and histones during nucleosome sliding and provides the structural basis for DNA translocation. ATP hydrolysis induces conformational changes in SNF2H that pull the DNA tracking strand, distorting DNA and histones at SHL2. This is followed by SNF2H rotation on the nucleosome, which first pulls the DNA guide strand and creates one-base pair bulge at SHL2, and then releases the pulled DNA. Given the high conservation of the catalytic motors among ATP-dependent chromatin remodelers, the mechanisms we describe likely apply to other families. |
リンク | bioRxiv / PubMed:39803580 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.6 - 4.2 Å |
| 構造データ | EMDB-47425, PDB-9e1y: ![]() EMDB-47427: SNF2H bound to nucleosome - Class E1 ![]() EMDB-47428: SNF2H bound to nucleosome - Class E2 |
| 由来 |
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キーワード | DNA BINDING PROTEIN/DNA / Chromatin / remodelers / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex |
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