Viral Nucleosome-Like Particles Exhibit Dynamic Flexibility and Reduced Thermodynamic Stability.

ABSTRACT: DNA packaging imposes fundamental physical constraints on genomes across the tree of life. However, most of our mechanistic understanding of these processes comes from the eukaryotic nucleosome, where highly basic histones, along with their flexible tails, coordinate DNA compaction and gene accessibility. Large DNA viruses challenge this paradigm by assembling nucleosome-like particles with a divergent histone architecture. These viral assemblies lack canonical histone tails, contain covalently fused domains linked by structured connectors, and exhibit altered surface electrostatics, features that collectively impose unique biophysical properties on viral chromatin. Here, we use multi-microsecond all-atom molecular dynamics simulations to dissect how histone fusion, tail loss, and connecto

SUBMITTER: Melo M 

PROVIDER: S-EPMC12330702 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature