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Roles of histone chaperone Nap1 and histone acetylation in regulating phase-separation of nucleosome arrays

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  • Jia Gao

    (The Pennsylvania State University, Department of Chemistry)

  • Hongyun Li

    (The Pennsylvania State University, Department of Chemistry)

  • Song Tan

    (The Pennsylvania State University, Department of Biochemistry and Molecular Biology)

  • Ruobo Zhou

    (The Pennsylvania State University, Department of Chemistry
    The Pennsylvania State University, Department of Biochemistry and Molecular Biology)

  • Tae-Hee Lee

    (The Pennsylvania State University, Department of Chemistry)

Abstract

Chromatin condensation is dynamically regulated throughout the cell cycle and plays key roles in modulating gene accessibility. The DNA-histone dynamics in the nucleosome are central to the regulation mechanisms of chromatin condensation, which remain poorly understood. Employing fluorescence recovery after photobleaching, optical super-resolution imaging, and microrheology with optical tweezers, we investigated the roles of various parameters in regulating phase-separation of 12-mer nucleosome arrays. Here, we show that histone H4 tail lysine residues are the main drivers of liquid-liquid phase separation of nucleosome arrays. We also show that the condensed liquid-like droplets comprise a mobile fraction and a relatively immobile structural scaffold. Histone chaperone Nap1 and histone H3 tail acetylation enhance DNA-histone dynamics within this scaffold, thereby lowering the overall viscosity of the droplets. These results suggest that histone chaperone and histone H3/H4 tails play critical roles in regulating chromatin condensation and gene accessibility in condensed chromatin.

Suggested Citation

  • Jia Gao & Hongyun Li & Song Tan & Ruobo Zhou & Tae-Hee Lee, 2025. "Roles of histone chaperone Nap1 and histone acetylation in regulating phase-separation of nucleosome arrays," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-65701-3
    DOI: 10.1038/s41467-025-65701-3
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