Melbournevirus-encoded histone doublets are recruited to virus particles and form destabilized nucleosome-like structures Journal Article uri icon

Overview

abstract

  • SummaryThe organization of genomic DNA into defined nucleosomes has long been viewed as a hallmark of eukaryotes. This paradigm has been challenged by the identification of ‘minimalist’ histones in archaea, and more recently by the discovery of genes that encode fused remote homologs of the four eukaryotic histones inMarseilleviridae, a subfamily of giant viruses that infect amoebae. We demonstrate that viral doublet histones localize to the cytoplasmic viral factories after virus infection, and ultimately to mature virions. CryoEM structures of viral nucleosome-like particles show strong similarities to eukaryotic nucleosomes, despite the limited sequence identify. The unique connectors that link the histone chains contribute to the observed instability of viral nucleosomes, and some histone tails assume structural roles. Our results further expand the range of ‘organisms’ that have nucleosomes and suggest a specialized function of histones in the biology of these unusual viruses.One Sentence SummarySome large DNA viruses encode fused histone doublets that are targeted to viral factories and assemble into open nucleosome-like structures.

publication date

  • April 29, 2021

has restriction

  • green

Date in CU Experts

  • April 30, 2021 10:05 AM

Full Author List

  • Liu Y; Toner CM; Philippe N; Jeudy S; Zhou K; Bowerman S; White A; Edwards G; Abergel C; Luger K

author count

  • 10

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