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9QV6

Asgard HHoB hypernucleosome in the closed state

Summary for 9QV6
Entry DOI10.2210/pdb9qv6/pdb
Related9QV5 9QV6 9QV7
EMDB information53386 53387 53388 53389 53390
DescriptorArchaeal histone A, DNA (180-MER) (3 entities in total)
Functional Keywordsarchaea, asgard, chromatin, histone, dna, nucleosome, dna binding protein
Biological sourceCandidatus Heimdallarchaeota archaeon LC_3
More
Total number of polymer chains14
Total formula weight204707.57
Authors
Ranawat, H.M.,Dodonova, S.O. (deposition date: 2025-04-11, release date: 2025-10-29, Last modification date: 2025-12-03)
Primary citationRanawat, H.M.,Cajili, M.K.,Lopez-Barbosa, N.,Quail, T.,Dame, R.T.,Dodonova, S.O.
Cryo-EM reveals open and closed Asgard chromatin assemblies.
Mol.Cell, 85:4152-, 2025
Cited by
PubMed Abstract: Asgards are the closest archaeal relatives of eukaryotes, representing an important step in chromatin evolution. However, their chromatin organization has remained enigmatic until now. In this study, we present the first structures of Asgard chromatin assemblies formed by the Hodarchaeal histone HHoB. Our high-resolution cryo-electron microscopy (cryo-EM) structures reveal that this Asgard histone assembles into compact "closed" and into extended "open" hypernucleosomes. Thus, the closed hypernucleosome conformation is conserved across archaeal lineages, while the open conformation resembles a eukaryotic H3-H4 octasome and likely represents an Asgard-specific innovation. Moreover, we show that Mg²⁺ ions influence Asgard chromatin conformation, suggesting a regulatory role. Overall, our study provides the first structure-based model of Asgard chromatin organization, expanding our understanding of chromatin architecture in an evolutionary context.
PubMed: 41161312
DOI: 10.1016/j.molcel.2025.10.001
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.6 Å)
Structure validation

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