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| Title | Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif. |
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| Journal, issue, pages | Genes Dev, Vol. 39, Issue 19-20, Page 1155-1161, Year 2025 |
| Publish date | Oct 1, 2025 |
Authors | Jaime Alegrio-Louro / Grisel Cruz-Becerra / George A Kassavetis / James T Kadonaga / Andres E Leschziner / ![]() |
| PubMed Abstract | The tardigrade damage suppressor (Dsup) and vertebrate high-mobility group N (HMGN) proteins bind specifically to nucleosomes via a conserved motif whose structure has not been experimentally ...The tardigrade damage suppressor (Dsup) and vertebrate high-mobility group N (HMGN) proteins bind specifically to nucleosomes via a conserved motif whose structure has not been experimentally determined. Here we used cryo-EM to show that both proteins bind to the nucleosome acidic patch via analogous arginine anchors with one molecule bound to each face of the nucleosome. We additionally used the natural promoter-containing 5S rDNA sequence for structural analysis of the nucleosome. These structures of an ancient nucleosome-binding motif suggest that there is an untapped realm of proteins with a related mode of binding to chromatin. |
External links | Genes Dev / PubMed:40721296 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.5 - 3.3 Å |
| Structure data | EMDB-46536, PDB-9d3k: EMDB-46537, PDB-9d3l: EMDB-46538, PDB-9d3m: EMDB-46540, PDB-9d3n: EMDB-46542, PDB-9d3o: EMDB-46543, PDB-9d3p: EMDB-46544, PDB-9d3q: EMDB-46545, PDB-9d3r: EMDB-46546, PDB-9d3s: EMDB-46547, PDB-9d3t: |
| Source |
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Keywords | GENE REGULATION/DNA / Dsup / nucleosome / tardigrade damage supressor protein / GENE REGULATION / GENE REGULATION-DNA complex / high mobility group N proteins (HMGN proteins) / HMGN2 / non-histone chromosomal proteins / 5S rDNA nucleosome / natural nucleosome positioning sequence / glutaraldehyde / cross-linking / DNA sequence-dependent breathing |
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homo sapiens (human)
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