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Cited by 5Genomics and Chromatin DynamicsBacteriophages and microbial interactionsDNA and Nucleic Acid Chemistry

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Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures

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Villalta, Alejandro, Bisio, Hugo, Toner, Chelsea M., Abergel, Chantal, Luger, Karolin·2025·Nature Communications
DOI 10.1038/s41467-025-62031-2PMC PMC12297534

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Abstract

Unique among viruses, some giant viruses utilize histones to organize their genomes into nucleosomes. Melbournevirus encodes a distinct H2B-H2A histone doublet variant in addition to the canonical H4-H3 and H2B-H2A doublets. This viral histone variant has a truncated H2B portion and its amino acid sequence deviates from that of the main viral H2B-H2A throughout the entire coding region. It is less abundant than the main H2B-H2A doublet, is likely essential for melbournevirus fitness, and is conserved in all Marseilleviridae . The cryo-EM structure of a nucleosome-like particle reconstituted with this H2B-H2A variant and viral H4-H3 reveals that only 90 base pairs of DNA are stably bound, significantly less than in eukaryotic nucleosomes and viral nucleosomes made with the main fused viral histone doublets. The reduced ability to bind DNA can be attributed to structural differences between variant and main H2B-H2A. Variant melbournevirus nucleosomes are less stable, possibly aiding rapid genome unpacking to initiate gene expression. Our results highlight the remarkable propensity of giant viruses to appropriate the utility of histones for their specialized purposes.

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Metadata

Authors
Villalta, A., Bisio, H., Toner, C. M., Abergel, C., & Luger, K.
Affiliations
  • Howard Hughes Medical Institute (US)
  • Centre National de la Recherche Scientifique (FR)
  • University of Colorado Boulder (US)
Corresponding author
Luger, Karolin
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2025-07-26
Volume
16
Issue
1
Pages
6903-6903
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-025-62031-2
PMC
PMC12297534
OpenAlex
W4412656177
Cited by
5
References
2
Citations by year
2026: 2 · 2025: 3
FWCI
1.50
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Science Foundation (1925766)
  • Howard Hughes Medical Institute
  • European Commission (HORIZON2020, 832601)
  • University of Colorado Boulder
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords
Marseilleviridae, giant viruses, histone variants, nucleosome structure, DNA binding, nucleosome stability, genome packaging, histone evolution
MeSH terms
Amino Acid Sequence, DNA, Viral, Histones, Nucleosomes, Viral Proteins, Genome, Viral, Cryoelectron Microscopy

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