ArticleBiochemistry2011
The divalent cations Ca2+ and Mg2+ play specific roles in stabilizing histone-DNA interactions within nucleosomes that are partially redundant with the core histone tail domains.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Free energy spectroscopy reveals the mechanistic landscape of chromatin compaction.Nucleic acids research · 2026Article
- Magnesium as a conformational gatekeeper of KRAS: Structural dynamics and therapeutic implications.Protein science : a publication of the Protein Society · 2026Article
- Differential presence of neutrophil extracellular traps in serum vs plasma of patients with critical limb-threatening ischemia.Research and practice in thrombosis and haemostasis · 2026Article
- Selective binding of divalent cations reshapes nucleosome mechanics and unlocks histone tail dynamics.Communications biology · 2026Article
- Free energy spectroscopy reveals the mechanistic landscape of chromatin compaction.bioRxiv : the preprint server for biology · 2025Article
- Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes.Journal of molecular biology · 2023Article
- Regulation associated modules reflect 3D genome modularity associated with chromatin activity.Nature communications · 2022Article
- Quantitative Analysis of the Interactions of Metal Complexes and Amphiphilic Systems: Calorimetric, Spectroscopic and Theoretical Aspects.Biomolecules · 2022Review
- Quantitative Modeling of Nucleosome Unwrapping from Both Ends.Biophysical journal · 2019Article
- Acetylation of the histone H3 tail domain regulates base excision repair on higher-order chromatin structures.Scientific reports · 2019Article
- Sequence-dependent nucleosome nanoscale structure characterized by atomic force microscopy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Epigenome Interactions with Patterned Neuronal Activity.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2018Review
- Calcium ions function as a booster of chromosome condensation.Scientific reports · 2016Article
- TRF1 and TRF2 binding to telomeres is modulated by nucleosomal organization.Nucleic acids research · 2015Article
- Cooperative stabilization of Zn(2+):DNA complexes through netropsin binding in the minor groove of FdU-substituted DNA.Journal of biomolecular structure & dynamics · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We previously reported that reconstituted nucleosomes undergo sequence-dependent translational repositioning upon removal of the core histone tail domains under physiological conditions, indicating that the tails influence the choice of position. We report here that removal of the core histone tail domains increases the exposure of the DNA backbone in nucleosomes to hydroxyl radicals, a nonbiased chemical cleavage reagent, indicative of an increase in the motility of the DNA on the histone surface. Moreover, we demonstrate that the divalent cations Mg(2+) and Ca(2+) can replace the role of the tail domains with regard to stabilization of histone-DNA interactions within the nucleosome core and restrict repositioning of nucleosomes upon tail removal. However, when nucleosomes were incubated with Mg(2+) after tail removal, the original distribution of translational positions was not re-established, indicating that divalent cations increase the energy barrier between translational positions rather than altering the free energy differences between positions. Interestingly, other divalent cations such as Zn(2+), Fe(2+), Co(2+), and Mn(2+) had little or no effect on the stability of histone-DNA interactions within tailless nucleosomes. These results support the idea that specific binding sites for Mg(2+) and Ca(2+) ions exist within the nucleosome and play a critical role in nucleosome stability that is partially redundant with the core histone tail domains.
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