Selective binding of divalent cations reshapes nucleosome mechanics and unlocks histone tail dynamics

Divalent cations such as Mg<sup>2+</sup> and Ca<sup>2+</sup> are key modulators of chromatin architecture, yet their atomistic influence on nucleosome structure and histone tail dynamics remains elusive. Here, we present 81 microseconds of all-atom molecular dynamics (MD) simulations to dissect how these ions shape nucleosome dynamics and plasticity. We quantitively mapped the selective binding patterns of Mg<sup>2+</sup> and Ca<sup>2+</sup> in nucleosomes with and without histone tails, revealing distinct ion-nucleosome interactions. Notably, divalent ion binding reduces inter-gyre electrostatic repulsion, facilitates DNA gyre compaction, and increases nucleosome stiffness, as quantified by estimates of the Young's modulus and correlated motions within specific DNA regions. Importantly, ion binding weakens histone tail-DNA interactions and enhances tail mobility-particularly that of H3-potentially facilitating access by chromatin regulators and tail-mediated chromatin compaction. These findings reveal a dual role of divalent ions in modulating nucleosome plasticity while reinforcing histone tail dynamics, providing a mechanistic framework for understanding how ionic fluctuations influence gene accessibility and chromatin state.

Authors

Institutions

Publication Details

Journal
Communications Biology
Published
2026-02-05
DOI
https://doi.org/10.1038/s42003-026-09648-1
Primary Topic
Genomics and Chromatin Dynamics
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Selective binding of divalent cations reshapes nucleosome mechanics and unlocks histone tail dynamics

Gege Liu, Guanhua HU, Yunhui Peng, Houfang Zhang et al.
Communications Biology
Genomics and Chromatin Dynamics
article

Selective binding of divalent cations reshapes nucleosome mechanics and unlocks histone tail dynamics

Gege Liu, Guanhua HU, Yunhui Peng, Houfang Zhang, Wang Xu
article en

Abstract

Divalent cations such as Mg<sup>2+</sup> and Ca<sup>2+</sup> are key modulators of chromatin architecture, yet their atomistic influence on nucleosome structure and histone tail dynamics remains elusive. Here, we present 81 microseconds of all-atom molecular dynamics (MD) simulations to dissect how these ions shape nucleosome dynamics and plasticity. We quantitively mapped the selective binding patterns of Mg<sup>2+</sup> and Ca<sup>2+</sup> in nucleosomes with and without histone tails, revealing distinct ion-nucleosome interactions. Notably, divalent ion binding reduces inter-gyre electrostatic repulsion, facilitates DNA gyre compaction, and increases nucleosome stiffness, as quantified by estimates of the Young's modulus and correlated motions within specific DNA regions. Importantly, ion binding weakens histone tail-DNA interactions and enhances tail mobility-particularly that of H3-potentially facilitating access by chromatin regulators and tail-mediated chromatin compaction. These findings reveal a dual role of divalent ions in modulating nucleosome plasticity while reinforcing histone tail dynamics, providing a mechanistic framework for understanding how ionic fluctuations influence gene accessibility and chromatin state.

Communications BiologyVol. 9(1)
Central China Normal University (CN), Institute of Biophysics (CN)
National Natural Science Foundation of China, Ministry of Education, India, Central China Normal University
Openalex Percentile: Top 66%
Genomics and Chromatin Dynamics
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.