ArticleCommunications biology2026
Linker histone H1 represses H3 tail acetylation induced by H4 tail acetylation and alters its dynamics.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed.
- Dynamic networks of intrinsically disordered regions in nuclear proteins.Biophysics and physicobiology · 2026Article
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11 authors.
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Abstract
The nucleosome is the fundamental chromatin unit, containing two copies of histones H2A, H2B, H3, and H4 wrapped by ~ 146 bp of core DNA plus linker DNA; addition of linker histone H1 forms a chromatosome. Tetra-acetylation of the H4 N-terminal tail (H4-4Kac) enhances H3 N-tail acetylation by altering their mutual dynamics, but how H1 influences these dynamics remains unclear. Using cryo-electron microscopy and coarse-grained molecular dynamics simulations, we show that H4-4Kac and unmodified chromatosomes share essentially identical core histone-DNA structures and similar H3 N-tail dynamics. However, nuclear magnetic resonance spectroscopy reveals that in the H4-4Kac chromatosome, the H3 N-tail adopts a dynamically robust DNA-contact state distinct from that in the unmodified chromatosome, resulting in markedly reduced H3 N-tail acetylation. These findings suggest that linker histone H1 suppresses the progression of euchromatin formation.
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