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-Structure paper
| Title | Structural characterisation of chromatin remodelling intermediates supports linker DNA dependent product inhibition as a mechanism for nucleosome spacing. |
|---|---|
| Journal, issue, pages | Elife, Vol. 14, Year 2025 |
| Publish date | Dec 24, 2025 |
Authors | Amanda L Hughes / Ramasubramanian Sundaramoorthy / Tom Owen-Hughes / ![]() |
| PubMed Abstract | Previously we showed that Chd1 chromatin remodelling enzyme associates with nucleosomes oriented towards the longer linker (Sundaramoorthy et al., 2018) (1). Here we report a series of structures of ...Previously we showed that Chd1 chromatin remodelling enzyme associates with nucleosomes oriented towards the longer linker (Sundaramoorthy et al., 2018) (1). Here we report a series of structures of Chd1 bound to nucleosomes during ongoing ATP-dependent repositioning. Combining these with biochemical experiments and existing literature we propose a model in which Chd1 first associates oriented to sample putative entry DNA. In an ATP-dependent reaction, the enzyme then redistributes to the opposite side of the nucleosome, where it subsequently adopts a conformation productive for DNA translocation. Once this active complex extends nascent exit linker to approximately 15bp, it is sensed by the Chd1 DNA binding domain resulting in conversion to a product inhibited state. These observations provide a mechanistic basis for the action of a molecular ruler element in nucleosome spacing. |
External links | Elife / PubMed:41439750 |
| Methods | EM (single particle) |
| Resolution | 3.8 - 4.2 Å |
| Structure data | EMDB-53590, PDB-9r5k: EMDB-53595, PDB-9r5s: |
| Source |
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Keywords | GENE REGULATION / Nucleosome / Remodelling enzyme |
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