Summary information and primary citation
- PDB-id
-
9d3q;
DSSR-derived features in text and
JSON formats
- Class
- gene regulation
- Method
- cryo-EM (2.8 Å)
- Summary
- 167-bp 5s rDNA nucleosome - open ii
- Reference
-
Alegrio-Louro J, Cruz-Becerra G, Kassavetis GA, Kadonaga
JT, Leschziner AE (2025): "Structural
basis of nucleosome recognition by the conserved Dsup and
HMGN nucleosome-binding motif." Genes Dev.,
39, 1155-1161. doi: 10.1101/gad.352720.125.
- 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 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.
