ArticleNature communications2024
Characterization of Medusavirus encoded histones reveals nucleosome-like structures and a unique linker histone.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Viral nucleosome-like particles show increased dynamic behavior and altered thermodynamic stability.Biophysical journal · 2026Article
- Integrative structural interactomics reveals protein organization and structure in a giant virus.Nature communications · 2026Article
- The double histone fold: Structure, functional implications across the tree of life and relevance to protein design.Protein science : a publication of the Protein Society · 2026Review
- TFAM organizes DNA into compact higher order structures.bioRxiv : the preprint server for biology · 2026Article
- Histone diversity in the archaeal domain of life.Nature communications · 2026Article
- A newly isolated giant virus, ushikuvirus, is closely related to clandestinovirus and shows a unique capsid surface structure and host cell interactions.Journal of virology · 2025Article
- Usurpativirus massiliensis, a new giant virus related to clandestinovirus.Virology journal · 2025Article
- Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures.Nature communications · 2025Article
- 20 years of research on giant viruses.Npj viruses · 2025Review
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Authors and funding
4 authors.
Funding
Abstract
The organization of DNA into nucleosomes is a ubiquitous and ancestral feature that was once thought to be exclusive to the eukaryotic domain of life. Intriguingly, several representatives of the Nucleocytoplasmic Large DNA Viruses (NCLDV) encode histone-like proteins that in Melbournevirus were shown to form nucleosome-like particles. Medusavirus medusae (MM), a distantly related giant virus, encodes all four core histone proteins and, unique amongst most giant viruses, a putative acidic protein with two domains resembling eukaryotic linker histone H1. Here, we report the structure of nucleosomes assembled with MM histones and highlight similarities and differences with eukaryotic and Melbournevirus nucleosomes. Our structure provides insight into how variations in histone tail and loop lengths are accommodated within the context of the nucleosome. We show that MM-histones assemble into tri-nucleosome arrays, and that the putative linker histone H1 does not function in chromatin compaction. These findings expand our limited understanding of chromatin organization by virus-encoded histones.
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